---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
PlanS_conform: '1'
_id: '20077'
abstract:
- lang: eng
text: Hyaluronic acid (HA) is a key extracellular matrix component of vertebrates,
where it mediates cell adhesion, immune regulation, and tissue remodeling through
its interaction with specific receptors. Although HA has been detected in a few
invertebrate species, the lack of fundamental components of the molecular HA pathway
poses relevant objections about its functional role in these species. Mining genomic
and transcriptomic data, we considered the conservation of the gene locus encoding
for the extracellular link protein (XLINK) in marine mussels as well as its expression
patterns. Structural and phylogenetic analyses were undertaken to evaluate possible
similarities with vertebrate orthologs and to infer the origin of this gene in
invertebrates. Biochemical analysis was used to quantify HA in tissues of Mytilus
galloprovincialis. As a result, we confirm that the mussel can produce HA (up
to 1.02 ng/mg in mantle) and that its genome encodes two XLINK gene loci. These
loci are conserved in Mytilidae species and show a complex evolutionary path.
Mussel XLINK genes appeared to be expressed during developmental stages in three
mussel species, ranking in the top 100 expressed genes in M. trossulus at 17 h
post-fertilization. In conclusion, the presence of HA and an active gene with
the potential to bind HA suggests that mussels have the potential to synthesize
and use HA and are among the few invertebrates encoding this gene.
acknowledgement: 'This research was funded by the Italian Ministry of University and
Research (MIUR), grant ID: P2022JEEMT (Developing a tool for the study of haplotype
diversity in Mytilus galloprovincialis (HAMIGA)).'
article_number: '930'
article_processing_charge: Yes
article_type: original
author:
- first_name: Umberto
full_name: Rosani, Umberto
last_name: Rosani
- first_name: Nehir
full_name: Altan, Nehir
last_name: Altan
- first_name: Paola
full_name: Venier, Paola
last_name: Venier
- first_name: Enrico
full_name: Bortoletto, Enrico
last_name: Bortoletto
- first_name: Nicola
full_name: Volpi, Nicola
last_name: Volpi
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
citation:
ama: Rosani U, Altan N, Venier P, Bortoletto E, Volpi N, Bernecky C. Ancestral origin
and functional expression of a hyaluronic acid pathway complement in mussels.
Biology. 2025;14(8). doi:10.3390/biology14080930
apa: Rosani, U., Altan, N., Venier, P., Bortoletto, E., Volpi, N., & Bernecky,
C. (2025). Ancestral origin and functional expression of a hyaluronic acid pathway
complement in mussels. Biology. MDPI. https://doi.org/10.3390/biology14080930
chicago: Rosani, Umberto, Nehir Altan, Paola Venier, Enrico Bortoletto, Nicola Volpi,
and Carrie Bernecky. “Ancestral Origin and Functional Expression of a Hyaluronic
Acid Pathway Complement in Mussels.” Biology. MDPI, 2025. https://doi.org/10.3390/biology14080930.
ieee: U. Rosani, N. Altan, P. Venier, E. Bortoletto, N. Volpi, and C. Bernecky,
“Ancestral origin and functional expression of a hyaluronic acid pathway complement
in mussels,” Biology, vol. 14, no. 8. MDPI, 2025.
ista: Rosani U, Altan N, Venier P, Bortoletto E, Volpi N, Bernecky C. 2025. Ancestral
origin and functional expression of a hyaluronic acid pathway complement in mussels.
Biology. 14(8), 930.
mla: Rosani, Umberto, et al. “Ancestral Origin and Functional Expression of a Hyaluronic
Acid Pathway Complement in Mussels.” Biology, vol. 14, no. 8, 930, MDPI,
2025, doi:10.3390/biology14080930.
short: U. Rosani, N. Altan, P. Venier, E. Bortoletto, N. Volpi, C. Bernecky, Biology
14 (2025).
date_created: 2025-07-25T08:28:26Z
date_published: 2025-07-24T00:00:00Z
date_updated: 2025-09-30T14:10:07Z
day: '24'
ddc:
- '570'
department:
- _id: CaBe
doi: 10.3390/biology14080930
external_id:
isi:
- '001557922100001'
file:
- access_level: open_access
checksum: f5e059e66803fa54249c1db029aef0f6
content_type: application/pdf
creator: dernst
date_created: 2025-07-31T09:11:09Z
date_updated: 2025-07-31T09:11:09Z
file_id: '20097'
file_name: 2025_Biology_Rosani.pdf
file_size: 1885781
relation: main_file
success: 1
file_date_updated: 2025-07-31T09:11:09Z
has_accepted_license: '1'
intvolume: ' 14'
isi: 1
issue: '8'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '07'
oa: 1
oa_version: Published Version
publication: Biology
publication_identifier:
issn:
- 2079-7737
publication_status: published
publisher: MDPI
quality_controlled: '1'
status: public
title: Ancestral origin and functional expression of a hyaluronic acid pathway complement
in mussels
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 14
year: '2025'
...
---
_id: '20804'
abstract:
- lang: eng
text: RNA polymerase II (Pol II) must be assembled in the cytoplasm before it enters
the nucleus, where it transcribes protein-coding genes. Although transcription
by Pol II is intensively studied, how this central multi-subunit enzyme is made
and the role of dedicated factors remains unclear. Here, we report the integrative
structural analysis of a native human Pol II from the cytoplasm captured near
the end of biogenesis. The complex contained Gdown1 and three biogenesis factors
– RPAP2 and the critical small GTPases GPN1 and GPN3. Cryo-EM analysis of the
complex revealed how Gdown1 and RPAP2 associate with Pol II and prevent the premature
association of transcription factors. Further biochemical and cryo-EM analysis
revealed how RPAP2 recruits GPN1–GPN3 to the complex, and how the assembly of
the RPAP2–GPN1–GPN3 complex is controlled by GTP hydrolysis. The combined results
uncover a network of interactions that chaperone cytoplasmic Pol II to prevent
aberrant interactions, reveal a GTP-controlled switch during the final stages
of Pol II biogenesis, and suggest a general mechanism for the action of GPN-loop
GTPase family of enzymes.
acknowledged_ssus:
- _id: LifeSc
- _id: EM-Fac
- _id: ScienComp
- _id: PreCl
acknowledgement: We thank A. Salmazo for assistance with Pol II purification. We thank
staff at the VBCF Proteomics facility for immunoprecipitation-mass spectrometry
analysis, and J.A. Stopp for assistance with IP-MS data visualization. This research
was further supported by the Scientific Service Units (SSUs) of IST Austria through
resources provided by the Lab Support Facility (LSF), Electron Microscopy (EMF),
Scientific Computing (SciComp), and the Preclinical Facility (PCF).
article_processing_charge: No
author:
- first_name: Annamaria
full_name: Hlavata, Annamaria
id: 36062FEC-F248-11E8-B48F-1D18A9856A87
last_name: Hlavata
- first_name: Benjamin
full_name: Neuditschko, Benjamin
last_name: Neuditschko
- first_name: Ulla
full_name: Schellhaas, Ulla
last_name: Schellhaas
- first_name: Clemens
full_name: Plaschka, Clemens
last_name: Plaschka
- first_name: Franz
full_name: Herzog, Franz
last_name: Herzog
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
citation:
ama: Hlavata A, Neuditschko B, Schellhaas U, Plaschka C, Herzog F, Bernecky C. Structure
of cytoplasmic RNA polymerase II. 2025. doi:10.64898/2025.12.10.692585
apa: Hlavata, A., Neuditschko, B., Schellhaas, U., Plaschka, C., Herzog, F., &
Bernecky, C. (2025). Structure of cytoplasmic RNA polymerase II. bioRxiv. https://doi.org/10.64898/2025.12.10.692585
chicago: Hlavata, Annamaria, Benjamin Neuditschko, Ulla Schellhaas, Clemens Plaschka,
Franz Herzog, and Carrie Bernecky. “Structure of Cytoplasmic RNA Polymerase II.”
bioRxiv, 2025. https://doi.org/10.64898/2025.12.10.692585.
ieee: A. Hlavata, B. Neuditschko, U. Schellhaas, C. Plaschka, F. Herzog, and C.
Bernecky, “Structure of cytoplasmic RNA polymerase II.” bioRxiv, 2025.
ista: Hlavata A, Neuditschko B, Schellhaas U, Plaschka C, Herzog F, Bernecky C.
2025. Structure of cytoplasmic RNA polymerase II. 10.64898/2025.12.10.692585.
mla: Hlavata, Annamaria, et al. Structure of Cytoplasmic RNA Polymerase II.
bioRxiv, 2025, doi:10.64898/2025.12.10.692585.
short: A. Hlavata, B. Neuditschko, U. Schellhaas, C. Plaschka, F. Herzog, C. Bernecky,
(2025).
corr_author: '1'
date_created: 2025-12-11T13:33:27Z
date_published: 2025-12-10T00:00:00Z
date_updated: 2025-12-15T09:48:22Z
day: '10'
department:
- _id: CaBe
doi: 10.64898/2025.12.10.692585
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.64898/2025.12.10.692585
month: '12'
oa: 1
oa_version: None
publication_status: published
publisher: bioRxiv
status: public
title: Structure of cytoplasmic RNA polymerase II
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2025'
...
---
APC_amount: 12348 EUR
OA_place: publisher
OA_type: hybrid
_id: '18778'
abstract:
- lang: eng
text: Transcription by RNA polymerase II (Pol II) can be repressed by noncoding
RNA, including the human RNA Alu. However, the mechanism by which endogenous RNAs
repress transcription remains unclear. Here we present cryogenic-electron microscopy
structures of Pol II bound to Alu RNA, which reveal that Alu RNA mimics how DNA
and RNA bind to Pol II during transcription elongation. Further, we show how distinct
domains of the general transcription factor TFIIF control repressive activity.
Together, we reveal how a noncoding RNA can regulate mammalian gene expression.
acknowledged_ssus:
- _id: LifeSc
- _id: EM-Fac
- _id: ScienComp
- _id: PreCl
acknowledgement: We thank the members of the Bernecky laboratory for helpful discussions
and A. Hlavata for providing Pol II for use in the fluorescence anisotropy binding
assay. We thank V.-V. Hodirnau for SerialEM data collection and support with EPU
data collection. We thank D. Slade (Max Perutz Laboratories and Medical University
of Vienna, Vienna, Austria) for the wild-type TFIIF expression plasmid. We thank
N. Thompson and R. Burgess (McArdle Laboratory for Cancer Research, University of
Wisconsin-Madison, Madison, WI, USA) for the 8WG16 hybridoma cell line. We thank
C. Plaschka and M. Loose for critical reading of the manuscript. This work was supported
by Austrian Science Fund (FWF) grant no. P34185 (DOI 10.55776/P34185) (C.B.). The
funders had no role in study design, data collection and analysis, decision to publish
or preparation of the manuscript. This research was further supported by the Scientific
Service Units of ISTA through resources provided by the Laboratory Support Facility,
Electron Microscopy Facility, Scientific Computing and the Preclinical Facility.
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Katarina
full_name: Tluckova, Katarina
id: 4AC7D980-F248-11E8-B48F-1D18A9856A87
last_name: Tluckova
- first_name: Beata M
full_name: Kaczmarek, Beata M
id: 36FA4AFA-F248-11E8-B48F-1D18A9856A87
last_name: Kaczmarek
- first_name: Anita P
full_name: Testa Salmazo, Anita P
id: 41F1F098-F248-11E8-B48F-1D18A9856A87
last_name: Testa Salmazo
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
citation:
ama: Tluckova K, Kaczmarek BM, Testa Salmazo AP, Bernecky C. Mechanism of mammalian
transcriptional repression by noncoding RNA. Nature Structural & Molecular
Biology. 2025;32:607-612. doi:10.1038/s41594-024-01448-7
apa: Tluckova, K., Kaczmarek, B. M., Testa Salmazo, A. P., & Bernecky, C. (2025).
Mechanism of mammalian transcriptional repression by noncoding RNA. Nature
Structural & Molecular Biology. Springer Nature. https://doi.org/10.1038/s41594-024-01448-7
chicago: Tluckova, Katarina, Beata M Kaczmarek, Anita P Testa Salmazo, and Carrie
Bernecky. “Mechanism of Mammalian Transcriptional Repression by Noncoding RNA.”
Nature Structural & Molecular Biology. Springer Nature, 2025. https://doi.org/10.1038/s41594-024-01448-7.
ieee: K. Tluckova, B. M. Kaczmarek, A. P. Testa Salmazo, and C. Bernecky, “Mechanism
of mammalian transcriptional repression by noncoding RNA,” Nature Structural
& Molecular Biology, vol. 32. Springer Nature, pp. 607–612, 2025.
ista: Tluckova K, Kaczmarek BM, Testa Salmazo AP, Bernecky C. 2025. Mechanism of
mammalian transcriptional repression by noncoding RNA. Nature Structural &
Molecular Biology. 32, 607–612.
mla: Tluckova, Katarina, et al. “Mechanism of Mammalian Transcriptional Repression
by Noncoding RNA.” Nature Structural & Molecular Biology, vol. 32,
Springer Nature, 2025, pp. 607–12, doi:10.1038/s41594-024-01448-7.
short: K. Tluckova, B.M. Kaczmarek, A.P. Testa Salmazo, C. Bernecky, Nature Structural
& Molecular Biology 32 (2025) 607–612.
corr_author: '1'
date_created: 2025-01-08T11:20:20Z
date_published: 2025-04-01T00:00:00Z
date_updated: 2025-11-20T10:28:36Z
day: '01'
ddc:
- '570'
department:
- _id: CaBe
doi: 10.1038/s41594-024-01448-7
external_id:
isi:
- '001390268000001'
pmid:
- '39762629'
file:
- access_level: open_access
checksum: 2919b30b271f395888e880076a680d73
content_type: application/pdf
creator: dernst
date_created: 2025-04-16T08:17:27Z
date_updated: 2025-04-16T08:17:27Z
file_id: '19573'
file_name: 2025_NatureStrucMolBiol_Tluckova.pdf
file_size: 9306639
relation: main_file
success: 1
file_date_updated: 2025-04-16T08:17:27Z
has_accepted_license: '1'
intvolume: ' 32'
isi: 1
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
page: 607-612
pmid: 1
project:
- _id: c08a6700-5a5b-11eb-8a69-82a722b2bc30
grant_number: P34185
name: Regulation of mammalian transcription by noncoding RNA
publication: Nature Structural & Molecular Biology
publication_identifier:
eissn:
- 1545-9985
issn:
- 1545-9993
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
record:
- id: '14644'
relation: earlier_version
status: public
scopus_import: '1'
status: public
title: Mechanism of mammalian transcriptional repression by noncoding RNA
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 32
year: '2025'
...
---
OA_type: closed access
_id: '19465'
article_number: '415'
article_processing_charge: No
article_type: letter_note
author:
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
citation:
ama: Bernecky C. Understanding the machinery that reads the genome. Nature Reviews
Molecular Cell Biology. 2025;26. doi:10.1038/s41580-025-00844-1
apa: Bernecky, C. (2025). Understanding the machinery that reads the genome. Nature
Reviews Molecular Cell Biology. Springer Nature. https://doi.org/10.1038/s41580-025-00844-1
chicago: Bernecky, Carrie. “Understanding the Machinery That Reads the Genome.”
Nature Reviews Molecular Cell Biology. Springer Nature, 2025. https://doi.org/10.1038/s41580-025-00844-1.
ieee: C. Bernecky, “Understanding the machinery that reads the genome,” Nature
Reviews Molecular Cell Biology, vol. 26. Springer Nature, 2025.
ista: Bernecky C. 2025. Understanding the machinery that reads the genome. Nature
Reviews Molecular Cell Biology. 26, 415.
mla: Bernecky, Carrie. “Understanding the Machinery That Reads the Genome.” Nature
Reviews Molecular Cell Biology, vol. 26, 415, Springer Nature, 2025, doi:10.1038/s41580-025-00844-1.
short: C. Bernecky, Nature Reviews Molecular Cell Biology 26 (2025).
corr_author: '1'
date_created: 2025-03-31T10:07:22Z
date_published: 2025-06-01T00:00:00Z
date_updated: 2025-09-30T11:20:36Z
day: '01'
department:
- _id: CaBe
doi: 10.1038/s41580-025-00844-1
external_id:
isi:
- '001455740100001'
pmid:
- '40155512'
intvolume: ' 26'
isi: 1
language:
- iso: eng
month: '06'
oa_version: None
pmid: 1
publication: Nature Reviews Molecular Cell Biology
publication_identifier:
eissn:
- 1471-0080
issn:
- 1471-0072
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Understanding the machinery that reads the genome
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 26
year: '2025'
...
---
OA_place: publisher
OA_type: hybrid
_id: '18553'
abstract:
- lang: eng
text: Transcription-coupled nucleotide excision repair (TC-NER) efficiently eliminates
DNA damage that impedes gene transcription by RNA polymerase II (RNA Pol II).
TC-NER is initiated by the recognition of lesion-stalled RNA Pol II by CSB, which
recruits the CRL4CSA ubiquitin ligase and UVSSA. RNA Pol II ubiquitylation at
RPB1-K1268 by CRL4CSA serves as a critical TC-NER checkpoint, governing RNA Pol
II stability and initiating DNA damage excision by TFIIH recruitment. However,
the precise regulatory mechanisms of CRL4CSA activity and TFIIH recruitment remain
elusive. Here, we reveal human serine/threonine-protein kinase 19 (STK19) as a
TC-NER factor, which is essential for correct DNA damage removal and subsequent
transcription restart. Cryogenic electron microscopy (cryo-EM) studies demonstrate
that STK19 is an integral part of the RNA Pol II-TC-NER complex, bridging CSA,
UVSSA, RNA Pol II, and downstream DNA. STK19 stimulates TC-NER complex stability
and CRL4CSA activity, resulting in efficient RNA Pol II ubiquitylation and correct
UVSSA and TFIIH binding. These findings underscore the crucial role of STK19 as
a core TC-NER component.
acknowledged_ssus:
- _id: LifeSc
- _id: PreCl
acknowledgement: We thank N. Thompson and R. Burgess for the 8WG16 hybridoma cell
line. This research was further supported by the Scientific Service Units (SSU)
of IST Austria through resources provided by the Lab Support Facility (LSF) and
the Preclinical Facility (PCF). This work is part of the Oncode Institute, which
is partly financed by the Dutch Cancer Society. Research at the Netherlands Cancer
Institute is supported by institutional grants of the Dutch Cancer Society and the
Dutch Ministry of Health, Welfare and Sport. This study was supported by a VICI
(VI.C.182.025) and a TOP Grant (714.017.003) of the Netherlands Organization for
Scientific Research.
article_processing_charge: No
article_type: original
author:
- first_name: Anisha R.
full_name: Ramadhin, Anisha R.
last_name: Ramadhin
- first_name: Shun-Hsiao
full_name: Lee, Shun-Hsiao
last_name: Lee
- first_name: Di
full_name: Zhou, Di
last_name: Zhou
- first_name: Anita P
full_name: Testa Salmazo, Anita P
id: 41F1F098-F248-11E8-B48F-1D18A9856A87
last_name: Testa Salmazo
- first_name: Camila
full_name: Gonzalo-Hansen, Camila
last_name: Gonzalo-Hansen
- first_name: Marjolein
full_name: van Sluis, Marjolein
last_name: van Sluis
- first_name: Cindy M.A.
full_name: Blom, Cindy M.A.
last_name: Blom
- first_name: Roel C.
full_name: Janssens, Roel C.
last_name: Janssens
- first_name: Anja
full_name: Raams, Anja
last_name: Raams
- first_name: Dick
full_name: Dekkers, Dick
last_name: Dekkers
- first_name: Karel
full_name: Bezstarosti, Karel
last_name: Bezstarosti
- first_name: Dea
full_name: Slade, Dea
last_name: Slade
- first_name: Wim
full_name: Vermeulen, Wim
last_name: Vermeulen
- first_name: Alex
full_name: Pines, Alex
last_name: Pines
- first_name: Jeroen A.A.
full_name: Demmers, Jeroen A.A.
last_name: Demmers
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Titia K.
full_name: Sixma, Titia K.
last_name: Sixma
- first_name: Jurgen A.
full_name: Marteijn, Jurgen A.
last_name: Marteijn
citation:
ama: Ramadhin AR, Lee S-H, Zhou D, et al. STK19 drives transcription-coupled repair
by stimulating repair complex stability, RNA Pol II ubiquitylation, and TFIIH
recruitment. Molecular Cell. 2024;84(24):4740-4757.e12. doi:10.1016/j.molcel.2024.10.030
apa: Ramadhin, A. R., Lee, S.-H., Zhou, D., Testa Salmazo, A. P., Gonzalo-Hansen,
C., van Sluis, M., … Marteijn, J. A. (2024). STK19 drives transcription-coupled
repair by stimulating repair complex stability, RNA Pol II ubiquitylation, and
TFIIH recruitment. Molecular Cell. Elsevier. https://doi.org/10.1016/j.molcel.2024.10.030
chicago: Ramadhin, Anisha R., Shun-Hsiao Lee, Di Zhou, Anita P Testa Salmazo, Camila
Gonzalo-Hansen, Marjolein van Sluis, Cindy M.A. Blom, et al. “STK19 Drives Transcription-Coupled
Repair by Stimulating Repair Complex Stability, RNA Pol II Ubiquitylation, and
TFIIH Recruitment.” Molecular Cell. Elsevier, 2024. https://doi.org/10.1016/j.molcel.2024.10.030.
ieee: A. R. Ramadhin et al., “STK19 drives transcription-coupled repair by
stimulating repair complex stability, RNA Pol II ubiquitylation, and TFIIH recruitment,”
Molecular Cell, vol. 84, no. 24. Elsevier, p. 4740–4757.e12, 2024.
ista: Ramadhin AR, Lee S-H, Zhou D, Testa Salmazo AP, Gonzalo-Hansen C, van Sluis
M, Blom CMA, Janssens RC, Raams A, Dekkers D, Bezstarosti K, Slade D, Vermeulen
W, Pines A, Demmers JAA, Bernecky C, Sixma TK, Marteijn JA. 2024. STK19 drives
transcription-coupled repair by stimulating repair complex stability, RNA Pol
II ubiquitylation, and TFIIH recruitment. Molecular Cell. 84(24), 4740–4757.e12.
mla: Ramadhin, Anisha R., et al. “STK19 Drives Transcription-Coupled Repair by Stimulating
Repair Complex Stability, RNA Pol II Ubiquitylation, and TFIIH Recruitment.” Molecular
Cell, vol. 84, no. 24, Elsevier, 2024, p. 4740–4757.e12, doi:10.1016/j.molcel.2024.10.030.
short: A.R. Ramadhin, S.-H. Lee, D. Zhou, A.P. Testa Salmazo, C. Gonzalo-Hansen,
M. van Sluis, C.M.A. Blom, R.C. Janssens, A. Raams, D. Dekkers, K. Bezstarosti,
D. Slade, W. Vermeulen, A. Pines, J.A.A. Demmers, C. Bernecky, T.K. Sixma, J.A.
Marteijn, Molecular Cell 84 (2024) 4740–4757.e12.
date_created: 2024-11-15T12:12:54Z
date_published: 2024-12-19T00:00:00Z
date_updated: 2025-09-08T14:42:50Z
day: '19'
ddc:
- '570'
department:
- _id: CaBe
doi: 10.1016/j.molcel.2024.10.030
external_id:
isi:
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date_created: 2025-01-13T11:17:35Z
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file_id: '18844'
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language:
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month: '12'
oa: 1
oa_version: Published Version
page: 4740-4757.e12
pmid: 1
publication: Molecular Cell
publication_identifier:
issn:
- 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: STK19 drives transcription-coupled repair by stimulating repair complex stability,
RNA Pol II ubiquitylation, and TFIIH recruitment
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 84
year: '2024'
...
---
_id: '14644'
abstract:
- lang: eng
text: Transcription by RNA polymerase II (Pol II) can be repressed by noncoding
RNA, including the human RNA Alu. However, the mechanism by which endogenous RNAs
repress transcription remains unclear. Here we present cryo-electron microscopy
structures of Pol II bound to Alu RNA, which reveal that Alu RNA mimics how DNA
and RNA bind to Pol II during transcription elongation. Further, we show how domains
of the general transcription factor TFIIF affect complex dynamics and control
repressive activity. Together, we reveal how a non-coding RNA can regulate mammalian
gene expression.
acknowledged_ssus:
- _id: LifeSc
- _id: EM-Fac
- _id: PreCl
acknowledgement: "We thank B. Kaczmarek and other members of the Bernecky lab for
helpful discussions. We thank V.-V. Hodirnau for SerialEM data collection and support
with EPU data collection. We thank D. Slade for the wild type TFIIF expression\r\nplasmid.
We thank N. Thompson and R. Burgess for the 8WG16 hybridoma cell line. We thank
C. Plaschka and M. Loose for critical reading of the manuscript. This work was supported
by Austrian Science Fund (FWF) grant P34185. This research was further supported
by the Scientific Service Units (SSU) of IST Austria through resources provided
by the Lab Support Facility (LSF), Electron Microscopy Facility (EMF), Scientific
Computing (SciComp), and the Preclinical Facility (PCF)."
article_processing_charge: No
author:
- first_name: Katarina
full_name: Tluckova, Katarina
id: 4AC7D980-F248-11E8-B48F-1D18A9856A87
last_name: Tluckova
- first_name: Anita P
full_name: Testa Salmazo, Anita P
id: 41F1F098-F248-11E8-B48F-1D18A9856A87
last_name: Testa Salmazo
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
citation:
ama: Tluckova K, Testa Salmazo AP, Bernecky C. Mechanism of mammalian transcriptional
repression by noncoding RNA. doi:10.15479/AT:ISTA:14644
apa: Tluckova, K., Testa Salmazo, A. P., & Bernecky, C. (n.d.). Mechanism of
mammalian transcriptional repression by noncoding RNA. Institute of Science and
Technology Austria. https://doi.org/10.15479/AT:ISTA:14644
chicago: Tluckova, Katarina, Anita P Testa Salmazo, and Carrie Bernecky. “Mechanism
of Mammalian Transcriptional Repression by Noncoding RNA.” Institute of Science
and Technology Austria, n.d. https://doi.org/10.15479/AT:ISTA:14644.
ieee: K. Tluckova, A. P. Testa Salmazo, and C. Bernecky, “Mechanism of mammalian
transcriptional repression by noncoding RNA.” Institute of Science and Technology
Austria.
ista: Tluckova K, Testa Salmazo AP, Bernecky C. Mechanism of mammalian transcriptional
repression by noncoding RNA. 10.15479/AT:ISTA:14644.
mla: Tluckova, Katarina, et al. Mechanism of Mammalian Transcriptional Repression
by Noncoding RNA. Institute of Science and Technology Austria, doi:10.15479/AT:ISTA:14644.
short: K. Tluckova, A.P. Testa Salmazo, C. Bernecky, (n.d.).
corr_author: '1'
date_created: 2023-12-04T14:51:00Z
date_published: 2023-12-05T00:00:00Z
date_updated: 2025-11-20T10:28:37Z
day: '05'
ddc:
- '572'
doi: 10.15479/AT:ISTA:14644
file:
- access_level: open_access
checksum: c45608cb97ee36d7b50ba518db8e07b0
content_type: application/pdf
creator: dernst
date_created: 2023-12-05T10:37:02Z
date_updated: 2023-12-05T10:37:02Z
file_id: '14646'
file_name: 2023_Tluckova_etal_REx.pdf
file_size: 4892920
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success: 1
file_date_updated: 2023-12-05T10:37:02Z
has_accepted_license: '1'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/4.0/
month: '12'
oa: 1
oa_version: Submitted Version
project:
- _id: c08a6700-5a5b-11eb-8a69-82a722b2bc30
grant_number: P34185
name: Regulation of mammalian transcription by noncoding RNA
publication_status: draft
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '18778'
relation: later_version
status: public
status: public
title: Mechanism of mammalian transcriptional repression by noncoding RNA
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '12051'
abstract:
- lang: eng
text: Transcription of the ribosomal RNA precursor by RNA polymerase (Pol) I is
a major determinant of cellular growth, and dysregulation is observed in many
cancer types. Here, we present the purification of human Pol I from cells carrying
a genomic GFP fusion on the largest subunit allowing the structural and functional
analysis of the enzyme across species. In contrast to yeast, human Pol I carries
a single-subunit stalk, and in vitro transcription indicates a reduced proofreading
activity. Determination of the human Pol I cryo-EM reconstruction in a close-to-native
state rationalizes the effects of disease-associated mutations and uncovers an
additional domain that is built into the sequence of Pol I subunit RPA1. This
“dock II” domain resembles a truncated HMG box incapable of DNA binding which
may serve as a downstream transcription factor–binding platform in metazoans.
Biochemical analysis, in situ modelling, and ChIP data indicate that Topoisomerase
2a can be recruited to Pol I via the domain and cooperates with the HMG box domain–containing
factor UBF. These adaptations of the metazoan Pol I transcription system may allow
efficient release of positive DNA supercoils accumulating downstream of the transcription
bubble.
acknowledgement: "The authors especially thank Philip Gunkel for his contribution.
We thank all\r\npast and present members of the Engel lab, Achim Griesenbeck, Colyn
Crane-\r\nRobinson, Christophe Lotz, Marlene Vayssieres, Klaus Grasser, Herbert
Tschochner, and Philipp Milkereit for help and discussion; Gerhard Lehmann and Nobert
Eichner for IT support; Joost Zomerdijk for UBF-constructs, Volker Cordes for the
Hela P2 cell line; Remco Sprangers for shared cell culture; Dina Grohmann and the
Archaea Center for fermentation; and Thomas\r\nDresselhaus for access to fluorescence
microscopes. This work was in part supported by the Emmy-Noether Programm (DFG grant
no. EN 1204/1-1 to C Engel) of the German Research Council and Collaborative Research
Center 960 (TP-A8 to C Engel)."
article_number: e202201568
article_processing_charge: No
article_type: original
author:
- first_name: Julia L
full_name: Daiß, Julia L
last_name: Daiß
- first_name: Michael
full_name: Pilsl, Michael
last_name: Pilsl
- first_name: Kristina
full_name: Straub, Kristina
last_name: Straub
- first_name: Andrea
full_name: Bleckmann, Andrea
last_name: Bleckmann
- first_name: Mona
full_name: Höcherl, Mona
last_name: Höcherl
- first_name: Florian B
full_name: Heiss, Florian B
last_name: Heiss
- first_name: Guillermo
full_name: Abascal-Palacios, Guillermo
last_name: Abascal-Palacios
- first_name: Ewan P
full_name: Ramsay, Ewan P
last_name: Ramsay
- first_name: Katarina
full_name: Tluckova, Katarina
id: 4AC7D980-F248-11E8-B48F-1D18A9856A87
last_name: Tluckova
- first_name: Jean-Clement
full_name: Mars, Jean-Clement
last_name: Mars
- first_name: Torben
full_name: Fürtges, Torben
last_name: Fürtges
- first_name: Astrid
full_name: Bruckmann, Astrid
last_name: Bruckmann
- first_name: Till
full_name: Rudack, Till
last_name: Rudack
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Valérie
full_name: Lamour, Valérie
last_name: Lamour
- first_name: Konstantin
full_name: Panov, Konstantin
last_name: Panov
- first_name: Alessandro
full_name: Vannini, Alessandro
last_name: Vannini
- first_name: Tom
full_name: Moss, Tom
last_name: Moss
- first_name: Christoph
full_name: Engel, Christoph
last_name: Engel
citation:
ama: Daiß JL, Pilsl M, Straub K, et al. The human RNA polymerase I structure reveals
an HMG-like docking domain specific to metazoans. Life Science Alliance.
2022;5(11). doi:10.26508/lsa.202201568
apa: Daiß, J. L., Pilsl, M., Straub, K., Bleckmann, A., Höcherl, M., Heiss, F. B.,
… Engel, C. (2022). The human RNA polymerase I structure reveals an HMG-like docking
domain specific to metazoans. Life Science Alliance. Life Science Alliance.
https://doi.org/10.26508/lsa.202201568
chicago: Daiß, Julia L, Michael Pilsl, Kristina Straub, Andrea Bleckmann, Mona Höcherl,
Florian B Heiss, Guillermo Abascal-Palacios, et al. “The Human RNA Polymerase
I Structure Reveals an HMG-like Docking Domain Specific to Metazoans.” Life
Science Alliance. Life Science Alliance, 2022. https://doi.org/10.26508/lsa.202201568.
ieee: J. L. Daiß et al., “The human RNA polymerase I structure reveals an
HMG-like docking domain specific to metazoans,” Life Science Alliance,
vol. 5, no. 11. Life Science Alliance, 2022.
ista: Daiß JL, Pilsl M, Straub K, Bleckmann A, Höcherl M, Heiss FB, Abascal-Palacios
G, Ramsay EP, Tluckova K, Mars J-C, Fürtges T, Bruckmann A, Rudack T, Bernecky
C, Lamour V, Panov K, Vannini A, Moss T, Engel C. 2022. The human RNA polymerase
I structure reveals an HMG-like docking domain specific to metazoans. Life Science
Alliance. 5(11), e202201568.
mla: Daiß, Julia L., et al. “The Human RNA Polymerase I Structure Reveals an HMG-like
Docking Domain Specific to Metazoans.” Life Science Alliance, vol. 5, no.
11, e202201568, Life Science Alliance, 2022, doi:10.26508/lsa.202201568.
short: J.L. Daiß, M. Pilsl, K. Straub, A. Bleckmann, M. Höcherl, F.B. Heiss, G.
Abascal-Palacios, E.P. Ramsay, K. Tluckova, J.-C. Mars, T. Fürtges, A. Bruckmann,
T. Rudack, C. Bernecky, V. Lamour, K. Panov, A. Vannini, T. Moss, C. Engel, Life
Science Alliance 5 (2022).
date_created: 2022-09-06T18:45:23Z
date_published: 2022-09-01T00:00:00Z
date_updated: 2024-10-21T06:01:48Z
day: '01'
ddc:
- '570'
department:
- _id: CaBe
doi: 10.26508/lsa.202201568
external_id:
isi:
- '000972702600001'
file:
- access_level: open_access
checksum: 4201d876a3e5e8b65e319d03300014ad
content_type: application/pdf
creator: dernst
date_created: 2022-09-08T06:41:14Z
date_updated: 2022-09-08T06:41:14Z
file_id: '12062'
file_name: 2022_LifeScienceAlliance_Daiss.pdf
file_size: 3183129
relation: main_file
success: 1
file_date_updated: 2022-09-08T06:41:14Z
has_accepted_license: '1'
intvolume: ' 5'
isi: 1
issue: '11'
keyword:
- Health
- Toxicology and Mutagenesis
- Plant Science
- Biochemistry
- Genetics and Molecular Biology (miscellaneous)
- Ecology
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
publication: Life Science Alliance
publication_identifier:
issn:
- 2575-1077
publication_status: published
publisher: Life Science Alliance
quality_controlled: '1'
scopus_import: '1'
status: public
title: The human RNA polymerase I structure reveals an HMG-like docking domain specific
to metazoans
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 5
year: '2022'
...
---
_id: '12143'
abstract:
- lang: eng
text: MicroRNA (miRNA) and RNA interference (RNAi) pathways rely on small RNAs produced
by Dicer endonucleases. Mammalian Dicer primarily supports the essential gene-regulating
miRNA pathway, but how it is specifically adapted to miRNA biogenesis is unknown.
We show that the adaptation entails a unique structural role of Dicer’s DExD/H
helicase domain. Although mice tolerate loss of its putative ATPase function,
the complete absence of the domain is lethal because it assures high-fidelity
miRNA biogenesis. Structures of murine Dicer⋅miRNA precursor complexes revealed
that the DExD/H domain has a helicase-unrelated structural function. It locks
Dicer in a closed state, which facilitates miRNA precursor selection. Transition
to a cleavage-competent open state is stimulated by Dicer-binding protein TARBP2.
Absence of the DExD/H domain or its mutations unlocks the closed state, reduces
substrate selectivity, and activates RNAi. Thus, the DExD/H domain structurally
contributes to mammalian miRNA biogenesis and underlies mechanistical partitioning
of miRNA and RNAi pathways.
acknowledged_ssus:
- _id: EM-Fac
acknowledgement: We thank Kristian Vlahovicek (University of Zagreb) for support of
bioinformatics analyses and Vladimir Benes (EMBL Sequencing Facility) and Genomics
and Bioinformatics Core Facility at the Institute of Molecular Genetics for help
with RNA sequencing. The main funding was provided by the Czech Science Foundation
(EXPRO grant 20-03950X to P.S. and 22-19896S to R. Stefl). Early stages of the work
were supported by European Research Council grants under the European Union’s Horizon
2020 Research and Innovation Programme (grants 647403 to P.S. and 649030 to R. Stefl).
V.B., D.F.J., and F.H. were in part supported by PhD student fellowships from the
Charles University; this work will be in part fulfilling requirements for a PhD
degree as “school work.” Funding of D.Z. included the OP RDE project “Internal Grant
Agency of Masaryk University” no. CZ.02.2.69/0.0/0.0/19_073/0016943. The Ministry
of Education, Youth, and Sports of the Czech Republic (MEYS CR) provided institutional
support for CEITEC 2020 project LQ1601. For technical support, we acknowledge EMBL
Monterotondo’s genome engineering and transgenic core facilities, the Czech Centre
for Phenogenomics at the Institute of Molecular Genetics (supported by RVO 68378050
from the Czech Academy of Sciences and LM2018126 and CZ.02.1.01/0.0/0.0/18_046/0015861
CCP Infrastructure Upgrade II from MEYS CR), the Cryo-EM and Proteomics Core Facilities
(CEITEC, Masaryk University) supported by the CIISB research infrastructure (LM2018127
from MEYS CR), and support from the Scientific Service Units of ISTA through resources
from the Electron Microscopy Facility. Computational resources included e-Infrastruktura
CZ (LM2018140) and ELIXIR-CZ (LM2018131) projects by MEYS CR and the Croatian National
Centres of Research Excellence in Personalized Healthcare (#KK.01.1.1.01.0010) and
Data Science and Advanced Cooperative Systems (#KK.01.1.1.01.0009) projects funded
by the European Structural and Investment Funds grants.
article_processing_charge: No
article_type: original
author:
- first_name: David
full_name: Zapletal, David
last_name: Zapletal
- first_name: Eliska
full_name: Taborska, Eliska
last_name: Taborska
- first_name: Josef
full_name: Pasulka, Josef
last_name: Pasulka
- first_name: Radek
full_name: Malik, Radek
last_name: Malik
- first_name: Karel
full_name: Kubicek, Karel
last_name: Kubicek
- first_name: Martina
full_name: Zanova, Martina
last_name: Zanova
- first_name: Christian
full_name: Much, Christian
last_name: Much
- first_name: Marek
full_name: Sebesta, Marek
last_name: Sebesta
- first_name: Valeria
full_name: Buccheri, Valeria
last_name: Buccheri
- first_name: Filip
full_name: Horvat, Filip
last_name: Horvat
- first_name: Irena
full_name: Jenickova, Irena
last_name: Jenickova
- first_name: Michaela
full_name: Prochazkova, Michaela
last_name: Prochazkova
- first_name: Jan
full_name: Prochazka, Jan
last_name: Prochazka
- first_name: Matyas
full_name: Pinkas, Matyas
last_name: Pinkas
- first_name: Jiri
full_name: Novacek, Jiri
last_name: Novacek
- first_name: Diego F.
full_name: Joseph, Diego F.
last_name: Joseph
- first_name: Radislav
full_name: Sedlacek, Radislav
last_name: Sedlacek
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Dónal
full_name: O’Carroll, Dónal
last_name: O’Carroll
- first_name: Richard
full_name: Stefl, Richard
last_name: Stefl
- first_name: Petr
full_name: Svoboda, Petr
last_name: Svoboda
citation:
ama: Zapletal D, Taborska E, Pasulka J, et al. Structural and functional basis of
mammalian microRNA biogenesis by Dicer. Molecular Cell. 2022;82(21):4064-4079.e13.
doi:10.1016/j.molcel.2022.10.010
apa: Zapletal, D., Taborska, E., Pasulka, J., Malik, R., Kubicek, K., Zanova, M.,
… Svoboda, P. (2022). Structural and functional basis of mammalian microRNA biogenesis
by Dicer. Molecular Cell. Elsevier. https://doi.org/10.1016/j.molcel.2022.10.010
chicago: Zapletal, David, Eliska Taborska, Josef Pasulka, Radek Malik, Karel Kubicek,
Martina Zanova, Christian Much, et al. “Structural and Functional Basis of Mammalian
MicroRNA Biogenesis by Dicer.” Molecular Cell. Elsevier, 2022. https://doi.org/10.1016/j.molcel.2022.10.010.
ieee: D. Zapletal et al., “Structural and functional basis of mammalian microRNA
biogenesis by Dicer,” Molecular Cell, vol. 82, no. 21. Elsevier, p. 4064–4079.e13,
2022.
ista: Zapletal D, Taborska E, Pasulka J, Malik R, Kubicek K, Zanova M, Much C, Sebesta
M, Buccheri V, Horvat F, Jenickova I, Prochazkova M, Prochazka J, Pinkas M, Novacek
J, Joseph DF, Sedlacek R, Bernecky C, O’Carroll D, Stefl R, Svoboda P. 2022. Structural
and functional basis of mammalian microRNA biogenesis by Dicer. Molecular Cell.
82(21), 4064–4079.e13.
mla: Zapletal, David, et al. “Structural and Functional Basis of Mammalian MicroRNA
Biogenesis by Dicer.” Molecular Cell, vol. 82, no. 21, Elsevier, 2022,
p. 4064–4079.e13, doi:10.1016/j.molcel.2022.10.010.
short: D. Zapletal, E. Taborska, J. Pasulka, R. Malik, K. Kubicek, M. Zanova, C.
Much, M. Sebesta, V. Buccheri, F. Horvat, I. Jenickova, M. Prochazkova, J. Prochazka,
M. Pinkas, J. Novacek, D.F. Joseph, R. Sedlacek, C. Bernecky, D. O’Carroll, R.
Stefl, P. Svoboda, Molecular Cell 82 (2022) 4064–4079.e13.
date_created: 2023-01-12T12:05:36Z
date_published: 2022-11-03T00:00:00Z
date_updated: 2023-08-04T08:57:17Z
day: '03'
ddc:
- '570'
department:
- _id: CaBe
doi: 10.1016/j.molcel.2022.10.010
external_id:
isi:
- '000898565300011'
pmid:
- '36332606'
file:
- access_level: open_access
checksum: 999e443b54e4fdaa2542ca5a97619731
content_type: application/pdf
creator: dernst
date_created: 2023-01-24T09:29:02Z
date_updated: 2023-01-24T09:29:02Z
file_id: '12354'
file_name: 2022_MolecularCell_Zapletal.pdf
file_size: 7368534
relation: main_file
success: 1
file_date_updated: 2023-01-24T09:29:02Z
has_accepted_license: '1'
intvolume: ' 82'
isi: 1
issue: '21'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
month: '11'
oa: 1
oa_version: Published Version
page: 4064-4079.e13
pmid: 1
publication: Molecular Cell
publication_identifier:
issn:
- 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structural and functional basis of mammalian microRNA biogenesis by Dicer
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 82
year: '2022'
...
---
_id: '10163'
abstract:
- lang: eng
text: The C-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol
II) is a regulatory hub for transcription and RNA processing. Here, we identify
PHD-finger protein 3 (PHF3) as a regulator of transcription and mRNA stability
that docks onto Pol II CTD through its SPOC domain. We characterize SPOC as a
CTD reader domain that preferentially binds two phosphorylated Serine-2 marks
in adjacent CTD repeats. PHF3 drives liquid-liquid phase separation of phosphorylated
Pol II, colocalizes with Pol II clusters and tracks with Pol II across the length
of genes. PHF3 knock-out or SPOC deletion in human cells results in increased
Pol II stalling, reduced elongation rate and an increase in mRNA stability, with
marked derepression of neuronal genes. Key neuronal genes are aberrantly expressed
in Phf3 knock-out mouse embryonic stem cells, resulting in impaired neuronal differentiation.
Our data suggest that PHF3 acts as a prominent effector of neuronal gene regulation
by bridging transcription with mRNA decay.
acknowledgement: 'D.S. thanks Claudine Kraft, Renée Schroeder, Verena Jantsch, Franz
Klein and Peter Schlögelhofer for support. We thank Anita Testa Salmazo for help
with purifying Pol II; Matthias Geyer and Robert Düster for sharing DYRK1A kinase;
Felix Hartmann and Clemens Plaschka for help with mass photometry; Goran Kokic for
design of the arrest assay sequences; Petra van der Lelij for help with generating
mESC KO; Maximilian Freilinger for help with the purification of mEGFP-CTD; Stefan
Ameres, Nina Fasching and Brian Reichholf for advice on SLAM-seq and for sharing
reagents; Laura Gallego Valle for advice regarding LLPS assays; Krzysztof Chylinski
for advice regarding CRISPR/Cas9 methodology; VBCF Protein Technologies facility
for purifying PHF3 and providing gRNAs and Cas9; VBCF NGS facility for sequencing;
Monoclonal antibody facility at the Helmholtz center for Pol II antibodies; Friedrich
Propst and Elzbieta Kowalska for advice and for sharing materials; Egon Ogris for
sharing materials; Martin Eilers for recommending a ChIP-grade TFIIS antibody; Susanne
Opravil, Otto Hudecz, Markus Hartl and Natascha Hartl for mass spectrometry analysis;
staff of the X-ray beamlines at the ESRF in Grenoble for their excellent support;
Christa Bücker, Anton Meinhart, Clemens Plaschka and members of the Slade lab for
critical comments on the manuscript; Life Science Editors for editing assistance.
M.B. and D.S. acknowledge support by the FWF-funded DK ‘Chromosome Dynamics’. T.K.
is a recipient of the DOC fellowship from the Austrian Academy of Sciences. U.S.
is supported by the L’Oreal for Women in Science Austria Fellowship and the Austrian
Science Fund (FWF T 795-B30). M.L is supported by the Vienna Science and Technology
Fund (WWTF, VRG14-006). R.S. is supported by the Czech Science Foundation (15-17670 S
and 21-24460 S), Ministry of Education, Youths and Sports of the Czech Republic
(CEITEC 2020 project (LQ1601)), and the European Research Council (ERC) under the
European Union’s Horizon 2020 research and innovation programme (Grant agreement
no. 649030); this publication reflects only the author’s view and the Research Executive
Agency is not responsible for any use that may be made of the information it contains.
M.S. is supported by the Czech Science Foundation (GJ20-21581Y). K.D.C. research
is supported by the Austrian Science Fund (FWF) Projects I525 and I1593, P22276,
P19060, and W1221, Federal Ministry of Economy, Family and Youth through the initiative
‘Laura Bassi Centres of Expertise’, funding from the Centre of Optimized Structural
Studies No. 253275, the Wellcome Trust Collaborative Award (201543/Z/16), COST action
BM1405 Non-globular proteins - from sequence to structure, function and application
in molecular physiopathology (NGP-NET), the Vienna Science and Technology Fund (WWTF
LS17-008), and by the University of Vienna. This project was funded by the MFPL
start-up grant, the Vienna Science and Technology Fund (WWTF LS14-001), and the
Austrian Science Fund (P31546-B28 and W1258 “DK: Integrative Structural Biology”)
to D.S.'
article_number: '6078'
article_processing_charge: No
article_type: original
author:
- first_name: Lisa-Marie
full_name: Appel, Lisa-Marie
last_name: Appel
- first_name: Vedran
full_name: Franke, Vedran
last_name: Franke
- first_name: Melania
full_name: Bruno, Melania
last_name: Bruno
- first_name: Irina
full_name: Grishkovskaya, Irina
last_name: Grishkovskaya
- first_name: Aiste
full_name: Kasiliauskaite, Aiste
last_name: Kasiliauskaite
- first_name: Tanja
full_name: Kaufmann, Tanja
last_name: Kaufmann
- first_name: Ursula E.
full_name: Schoeberl, Ursula E.
last_name: Schoeberl
- first_name: Martin G.
full_name: Puchinger, Martin G.
last_name: Puchinger
- first_name: Sebastian
full_name: Kostrhon, Sebastian
last_name: Kostrhon
- first_name: Carmen
full_name: Ebenwaldner, Carmen
last_name: Ebenwaldner
- first_name: Marek
full_name: Sebesta, Marek
last_name: Sebesta
- first_name: Etienne
full_name: Beltzung, Etienne
last_name: Beltzung
- first_name: Karl
full_name: Mechtler, Karl
last_name: Mechtler
- first_name: Gen
full_name: Lin, Gen
last_name: Lin
- first_name: Anna
full_name: Vlasova, Anna
last_name: Vlasova
- first_name: Martin
full_name: Leeb, Martin
last_name: Leeb
- first_name: Rushad
full_name: Pavri, Rushad
last_name: Pavri
- first_name: Alexander
full_name: Stark, Alexander
last_name: Stark
- first_name: Altuna
full_name: Akalin, Altuna
last_name: Akalin
- first_name: Richard
full_name: Stefl, Richard
last_name: Stefl
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Kristina
full_name: Djinovic-Carugo, Kristina
last_name: Djinovic-Carugo
- first_name: Dea
full_name: Slade, Dea
last_name: Slade
citation:
ama: Appel L-M, Franke V, Bruno M, et al. PHF3 regulates neuronal gene expression
through the Pol II CTD reader domain SPOC. Nature Communications. 2021;12(1).
doi:10.1038/s41467-021-26360-2
apa: Appel, L.-M., Franke, V., Bruno, M., Grishkovskaya, I., Kasiliauskaite, A.,
Kaufmann, T., … Slade, D. (2021). PHF3 regulates neuronal gene expression through
the Pol II CTD reader domain SPOC. Nature Communications. Springer Nature.
https://doi.org/10.1038/s41467-021-26360-2
chicago: Appel, Lisa-Marie, Vedran Franke, Melania Bruno, Irina Grishkovskaya, Aiste
Kasiliauskaite, Tanja Kaufmann, Ursula E. Schoeberl, et al. “PHF3 Regulates Neuronal
Gene Expression through the Pol II CTD Reader Domain SPOC.” Nature Communications.
Springer Nature, 2021. https://doi.org/10.1038/s41467-021-26360-2.
ieee: L.-M. Appel et al., “PHF3 regulates neuronal gene expression through
the Pol II CTD reader domain SPOC,” Nature Communications, vol. 12, no.
1. Springer Nature, 2021.
ista: Appel L-M, Franke V, Bruno M, Grishkovskaya I, Kasiliauskaite A, Kaufmann
T, Schoeberl UE, Puchinger MG, Kostrhon S, Ebenwaldner C, Sebesta M, Beltzung
E, Mechtler K, Lin G, Vlasova A, Leeb M, Pavri R, Stark A, Akalin A, Stefl R,
Bernecky C, Djinovic-Carugo K, Slade D. 2021. PHF3 regulates neuronal gene expression
through the Pol II CTD reader domain SPOC. Nature Communications. 12(1), 6078.
mla: Appel, Lisa-Marie, et al. “PHF3 Regulates Neuronal Gene Expression through
the Pol II CTD Reader Domain SPOC.” Nature Communications, vol. 12, no.
1, 6078, Springer Nature, 2021, doi:10.1038/s41467-021-26360-2.
short: L.-M. Appel, V. Franke, M. Bruno, I. Grishkovskaya, A. Kasiliauskaite, T.
Kaufmann, U.E. Schoeberl, M.G. Puchinger, S. Kostrhon, C. Ebenwaldner, M. Sebesta,
E. Beltzung, K. Mechtler, G. Lin, A. Vlasova, M. Leeb, R. Pavri, A. Stark, A.
Akalin, R. Stefl, C. Bernecky, K. Djinovic-Carugo, D. Slade, Nature Communications
12 (2021).
date_created: 2021-10-20T14:40:32Z
date_published: 2021-10-19T00:00:00Z
date_updated: 2024-10-21T06:02:05Z
day: '19'
ddc:
- '610'
department:
- _id: CaBe
doi: 10.1038/s41467-021-26360-2
external_id:
isi:
- '000709050300001'
file:
- access_level: open_access
checksum: d99fcd51aebde19c21314e3de0148007
content_type: application/pdf
creator: cchlebak
date_created: 2021-10-21T13:51:49Z
date_updated: 2021-10-21T13:51:49Z
file_id: '10169'
file_name: 2021_NatComm_Appel.pdf
file_size: 5111706
relation: main_file
success: 1
file_date_updated: 2021-10-21T13:51:49Z
has_accepted_license: '1'
intvolume: ' 12'
isi: 1
issue: '1'
keyword:
- general physics and astronomy
- general biochemistry
- genetics and molecular biology
- general chemistry
language:
- iso: eng
month: '10'
oa: 1
oa_version: Published Version
publication: Nature Communications
publication_identifier:
eissn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- description: 'Preprint '
relation: earlier_version
url: https://www.biorxiv.org/content/10.1101/2020.02.11.943159
scopus_import: '1'
status: public
title: PHF3 regulates neuronal gene expression through the Pol II CTD reader domain
SPOC
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 12
year: '2021'
...
---
_id: '600'
abstract:
- lang: eng
text: Transcription initiation at the ribosomal RNA promoter requires RNA polymerase
(Pol) I and the initiation factors Rrn3 and core factor (CF). Here, we combine
X-ray crystallography and cryo-electron microscopy (cryo-EM) to obtain a molecular
model for basal Pol I initiation. The three-subunit CF binds upstream promoter
DNA, docks to the Pol I-Rrn3 complex, and loads DNA into the expanded active center
cleft of the polymerase. DNA unwinding between the Pol I protrusion and clamp
domains enables cleft contraction, resulting in an active Pol I conformation and
RNA synthesis. Comparison with the Pol II system suggests that promoter specificity
relies on a distinct “bendability” and “meltability” of the promoter sequence
that enables contacts between initiation factors, DNA, and polymerase.
article_processing_charge: No
author:
- first_name: Christoph
full_name: Engel, Christoph
last_name: Engel
- first_name: Tobias
full_name: Gubbey, Tobias
last_name: Gubbey
- first_name: Simon
full_name: Neyer, Simon
last_name: Neyer
- first_name: Sarah
full_name: Sainsbury, Sarah
last_name: Sainsbury
- first_name: Christiane
full_name: Oberthuer, Christiane
last_name: Oberthuer
- first_name: Carlo
full_name: Baejen, Carlo
last_name: Baejen
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Patrick
full_name: Cramer, Patrick
last_name: Cramer
citation:
ama: Engel C, Gubbey T, Neyer S, et al. Structural basis of RNA polymerase I transcription
initiation. Cell. 2017;169(1):120-131.e22. doi:10.1016/j.cell.2017.03.003
apa: Engel, C., Gubbey, T., Neyer, S., Sainsbury, S., Oberthuer, C., Baejen, C.,
… Cramer, P. (2017). Structural basis of RNA polymerase I transcription initiation.
Cell. Cell Press. https://doi.org/10.1016/j.cell.2017.03.003
chicago: Engel, Christoph, Tobias Gubbey, Simon Neyer, Sarah Sainsbury, Christiane
Oberthuer, Carlo Baejen, Carrie Bernecky, and Patrick Cramer. “Structural Basis
of RNA Polymerase I Transcription Initiation.” Cell. Cell Press, 2017.
https://doi.org/10.1016/j.cell.2017.03.003.
ieee: C. Engel et al., “Structural basis of RNA polymerase I transcription
initiation,” Cell, vol. 169, no. 1. Cell Press, p. 120–131.e22, 2017.
ista: Engel C, Gubbey T, Neyer S, Sainsbury S, Oberthuer C, Baejen C, Bernecky C,
Cramer P. 2017. Structural basis of RNA polymerase I transcription initiation.
Cell. 169(1), 120–131.e22.
mla: Engel, Christoph, et al. “Structural Basis of RNA Polymerase I Transcription
Initiation.” Cell, vol. 169, no. 1, Cell Press, 2017, p. 120–131.e22, doi:10.1016/j.cell.2017.03.003.
short: C. Engel, T. Gubbey, S. Neyer, S. Sainsbury, C. Oberthuer, C. Baejen, C.
Bernecky, P. Cramer, Cell 169 (2017) 120–131.e22.
date_created: 2018-12-11T11:47:25Z
date_published: 2017-03-23T00:00:00Z
date_updated: 2025-09-11T07:38:07Z
day: '23'
doi: 10.1016/j.cell.2017.03.003
extern: '1'
external_id:
isi:
- '000397090000013'
intvolume: ' 169'
isi: 1
issue: '1'
language:
- iso: eng
month: '03'
oa_version: None
page: 120 - 131.e22
publication: Cell
publication_identifier:
issn:
- '00928674'
publication_status: published
publisher: Cell Press
publist_id: '7204'
quality_controlled: '1'
status: public
title: Structural basis of RNA polymerase I transcription initiation
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 169
year: '2017'
...
---
_id: '601'
abstract:
- lang: eng
text: 'The conserved polymerase-Associated factor 1 complex (Paf1C) plays multiple
roles in chromatin transcription and genomic regulation. Paf1C comprises the five
subunits Paf1, Leo1, Ctr9, Cdc73 and Rtf1, and binds to the RNA polymerase II
(Pol II) transcription elongation complex (EC). Here we report the reconstitution
of Paf1C from Saccharomyces cerevisiae, and a structural analysis of Paf1C bound
to a Pol II EC containing the elongation factor TFIIS. Cryo-electron microscopy
and crosslinking data reveal that Paf1C is highly mobile and extends over the
outer Pol II surface from the Rpb2 to the Rpb3 subunit. The Paf1-Leo1 heterodimer
and Cdc73 form opposite ends of Paf1C, whereas Ctr9 bridges between them. Consistent
with the structural observations, the initiation factor TFIIF impairs Paf1C binding
to Pol II, whereas the elongation factor TFIIS enhances it. We further show that
Paf1C is globally required for normal mRNA transcription in yeast. These results
provide a three-dimensional framework for further analysis of Paf1C function in
transcription through chromatin. '
article_number: '15741'
article_processing_charge: No
author:
- first_name: Youwei
full_name: Xu, Youwei
last_name: Xu
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Chung
full_name: Lee, Chung
last_name: Lee
- first_name: Kerstin
full_name: Maier, Kerstin
last_name: Maier
- first_name: Björn
full_name: Schwalb, Björn
last_name: Schwalb
- first_name: Dimitri
full_name: Tegunov, Dimitri
last_name: Tegunov
- first_name: Jürgen
full_name: Plitzko, Jürgen
last_name: Plitzko
- first_name: Henning
full_name: Urlaub, Henning
last_name: Urlaub
- first_name: Patrick
full_name: Cramer, Patrick
last_name: Cramer
citation:
ama: Xu Y, Bernecky C, Lee C, et al. Architecture of the RNA polymerase II-Paf1C-TFIIS
transcription elongation complex. Nature Communications. 2017;8. doi:10.1038/ncomms15741
apa: Xu, Y., Bernecky, C., Lee, C., Maier, K., Schwalb, B., Tegunov, D., … Cramer,
P. (2017). Architecture of the RNA polymerase II-Paf1C-TFIIS transcription elongation
complex. Nature Communications. Nature Publishing Group. https://doi.org/10.1038/ncomms15741
chicago: Xu, Youwei, Carrie Bernecky, Chung Lee, Kerstin Maier, Björn Schwalb, Dimitri
Tegunov, Jürgen Plitzko, Henning Urlaub, and Patrick Cramer. “Architecture of
the RNA Polymerase II-Paf1C-TFIIS Transcription Elongation Complex.” Nature
Communications. Nature Publishing Group, 2017. https://doi.org/10.1038/ncomms15741.
ieee: Y. Xu et al., “Architecture of the RNA polymerase II-Paf1C-TFIIS transcription
elongation complex,” Nature Communications, vol. 8. Nature Publishing Group,
2017.
ista: Xu Y, Bernecky C, Lee C, Maier K, Schwalb B, Tegunov D, Plitzko J, Urlaub
H, Cramer P. 2017. Architecture of the RNA polymerase II-Paf1C-TFIIS transcription
elongation complex. Nature Communications. 8, 15741.
mla: Xu, Youwei, et al. “Architecture of the RNA Polymerase II-Paf1C-TFIIS Transcription
Elongation Complex.” Nature Communications, vol. 8, 15741, Nature Publishing
Group, 2017, doi:10.1038/ncomms15741.
short: Y. Xu, C. Bernecky, C. Lee, K. Maier, B. Schwalb, D. Tegunov, J. Plitzko,
H. Urlaub, P. Cramer, Nature Communications 8 (2017).
date_created: 2018-12-11T11:47:25Z
date_published: 2017-06-06T00:00:00Z
date_updated: 2021-01-12T08:05:40Z
day: '06'
ddc:
- '570'
doi: 10.1038/ncomms15741
extern: '1'
file:
- access_level: open_access
checksum: 940742282a9a285dc4aeae0c2b5ebe96
content_type: application/pdf
creator: dernst
date_created: 2019-01-21T14:48:10Z
date_updated: 2020-07-14T12:47:16Z
file_id: '5865'
file_name: 2017_NatureComm_Xu.pdf
file_size: 3018075
relation: main_file
file_date_updated: 2020-07-14T12:47:16Z
has_accepted_license: '1'
intvolume: ' 8'
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
publication: Nature Communications
publication_identifier:
issn:
- '20411723'
publication_status: published
publisher: Nature Publishing Group
publist_id: '7203'
quality_controlled: '1'
status: public
title: Architecture of the RNA polymerase II-Paf1C-TFIIS transcription elongation
complex
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 8
year: '2017'
...
---
_id: '603'
abstract:
- lang: eng
text: During transcription, RNA polymerase II (Pol II) associates with the conserved
elongation factor DSIF. DSIF renders the elongation complex stable and functions
during Pol II pausing and RNA processing. We combined cryo-EM and X-ray crystallography
to determine the structure of the mammalian Pol II-DSIF elongation complex at
a nominal resolution of 3.4. Human DSIF has a modular structure with two domains
forming a DNA clamp, two domains forming an RNA clamp, and one domain buttressing
the RNA clamp. The clamps maintain the transcription bubble, position upstream
DNA, and retain the RNA transcript in the exit tunnel. The mobile C-terminal region
of DSIF is located near exiting RNA, where it can recruit factors for RNA processing.
The structure provides insight into the roles of DSIF during mRNA synthesis.
article_processing_charge: No
author:
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Jürgen
full_name: Plitzko, Jürgen
last_name: Plitzko
- first_name: Patrick
full_name: Cramer, Patrick
last_name: Cramer
citation:
ama: Bernecky C, Plitzko J, Cramer P. Structure of a transcribing RNA polymerase
II-DSIF complex reveals a multidentate DNA-RNA clamp. Nature Structural and
Molecular Biology. 2017;24(10):809-815. doi:10.1038/nsmb.3465
apa: Bernecky, C., Plitzko, J., & Cramer, P. (2017). Structure of a transcribing
RNA polymerase II-DSIF complex reveals a multidentate DNA-RNA clamp. Nature
Structural and Molecular Biology. Nature Publishing Group. https://doi.org/10.1038/nsmb.3465
chicago: Bernecky, Carrie, Jürgen Plitzko, and Patrick Cramer. “Structure of a Transcribing
RNA Polymerase II-DSIF Complex Reveals a Multidentate DNA-RNA Clamp.” Nature
Structural and Molecular Biology. Nature Publishing Group, 2017. https://doi.org/10.1038/nsmb.3465.
ieee: C. Bernecky, J. Plitzko, and P. Cramer, “Structure of a transcribing RNA polymerase
II-DSIF complex reveals a multidentate DNA-RNA clamp,” Nature Structural and
Molecular Biology, vol. 24, no. 10. Nature Publishing Group, pp. 809–815,
2017.
ista: Bernecky C, Plitzko J, Cramer P. 2017. Structure of a transcribing RNA polymerase
II-DSIF complex reveals a multidentate DNA-RNA clamp. Nature Structural and Molecular
Biology. 24(10), 809–815.
mla: Bernecky, Carrie, et al. “Structure of a Transcribing RNA Polymerase II-DSIF
Complex Reveals a Multidentate DNA-RNA Clamp.” Nature Structural and Molecular
Biology, vol. 24, no. 10, Nature Publishing Group, 2017, pp. 809–15, doi:10.1038/nsmb.3465.
short: C. Bernecky, J. Plitzko, P. Cramer, Nature Structural and Molecular Biology
24 (2017) 809–815.
date_created: 2018-12-11T11:47:26Z
date_published: 2017-10-05T00:00:00Z
date_updated: 2025-09-11T07:37:28Z
day: '05'
doi: 10.1038/nsmb.3465
extern: '1'
external_id:
isi:
- '000412278000007'
intvolume: ' 24'
isi: 1
issue: '10'
language:
- iso: eng
month: '10'
oa_version: None
page: 809 - 815
publication: Nature Structural and Molecular Biology
publication_identifier:
issn:
- '15459993'
publication_status: published
publisher: Nature Publishing Group
publist_id: '7202'
quality_controlled: '1'
status: public
title: Structure of a transcribing RNA polymerase II-DSIF complex reveals a multidentate
DNA-RNA clamp
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 24
year: '2017'
...
---
_id: '602'
abstract:
- lang: eng
text: RNA polymerase (Pol) II produces messenger RNA during transcription of protein-coding
genes in all eukaryotic cells. The Pol II structure is known at high resolution
from X-ray crystallography for two yeast species1-3. Structural studies of mammalian
Pol II, however, remain limited to low-resolution electron microscopy analysis
of human Pol II and its complexes with various proteins4-10. Here we report the
3.4 Å resolution cryo-electron microscopy structure of mammalian Pol II in the
form of a transcribing complex comprising DNA template and RNA transcript. We
use bovine Pol II, which is identical to the human enzyme except for seven amino-acid
residues. The obtained atomic model closely resembles its yeast counterpart, but
also reveals unknown features. Binding of nucleic acids to the polymerase involves
'induced fit' of the mobile Pol II clamp and active centre region. DNA downstream
of the transcription bubble contacts a conserved 'TPSA motif' in the jaw domain
of the Pol II subunit RPB5, an interaction that is apparently already established
during transcription initiation7. Upstream DNA emanates from the active centre
cleft at an angle of approximately 105° with respect to downstream DNA. This position
of upstream DNA allows for binding of the general transcription elongation factor
DSIF (SPT4-SPT5) that we localize over the active centre cleft in a conserved
position on the clamp domain of Pol II. Our results define the structure of mammalian
Pol II in its functional state, indicate that previous crystallographic analysis
of yeast Pol II is relevant for understanding gene transcription in all eukaryotes,
and provide a starting point for a mechanistic analysis of human transcription.
article_processing_charge: No
author:
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Franz
full_name: Herzog, Franz
last_name: Herzog
- first_name: Wolfgang
full_name: Baumeister, Wolfgang
last_name: Baumeister
- first_name: Jürgen
full_name: Plitzko, Jürgen
last_name: Plitzko
- first_name: Patrick
full_name: Cramer, Patrick
last_name: Cramer
citation:
ama: Bernecky C, Herzog F, Baumeister W, Plitzko J, Cramer P. Structure of transcribing
mammalian RNA polymerase II. Nature. 2016;529(7587):551-554. doi:10.1038/nature16482
apa: Bernecky, C., Herzog, F., Baumeister, W., Plitzko, J., & Cramer, P. (2016).
Structure of transcribing mammalian RNA polymerase II. Nature. Nature Publishing
Group. https://doi.org/10.1038/nature16482
chicago: Bernecky, Carrie, Franz Herzog, Wolfgang Baumeister, Jürgen Plitzko, and
Patrick Cramer. “Structure of Transcribing Mammalian RNA Polymerase II.” Nature.
Nature Publishing Group, 2016. https://doi.org/10.1038/nature16482.
ieee: C. Bernecky, F. Herzog, W. Baumeister, J. Plitzko, and P. Cramer, “Structure
of transcribing mammalian RNA polymerase II,” Nature, vol. 529, no. 7587.
Nature Publishing Group, pp. 551–554, 2016.
ista: Bernecky C, Herzog F, Baumeister W, Plitzko J, Cramer P. 2016. Structure of
transcribing mammalian RNA polymerase II. Nature. 529(7587), 551–554.
mla: Bernecky, Carrie, et al. “Structure of Transcribing Mammalian RNA Polymerase
II.” Nature, vol. 529, no. 7587, Nature Publishing Group, 2016, pp. 551–54,
doi:10.1038/nature16482.
short: C. Bernecky, F. Herzog, W. Baumeister, J. Plitzko, P. Cramer, Nature 529
(2016) 551–554.
date_created: 2018-12-11T11:47:26Z
date_published: 2016-01-28T00:00:00Z
date_updated: 2021-01-12T08:05:43Z
day: '28'
doi: 10.1038/nature16482
extern: '1'
intvolume: ' 529'
issue: '7587'
language:
- iso: eng
month: '01'
oa_version: None
page: 551 - 554
publication: Nature
publication_status: published
publisher: Nature Publishing Group
publist_id: '7205'
status: public
title: Structure of transcribing mammalian RNA polymerase II
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 529
year: '2016'
...
---
_id: '594'
abstract:
- lang: eng
text: Transcription of eukaryotic protein-coding genes commences with the assembly
of a conserved initiation complex, which consists of RNA polymerase II (Pol II)
and the general transcription factors, at promoter DNA. After two decades of research,
the structural basis of transcription initiation is emerging. Crystal structures
of many components of the initiation complex have been resolved, and structural
information on Pol II complexes with general transcription factors has recently
been obtained. Although mechanistic details await elucidation, available data
outline how Pol II cooperates with the general transcription factors to bind to
and open promoter DNA, and how Pol II directs RNA synthesis and escapes from the
promoter.
article_processing_charge: No
author:
- first_name: Sarah
full_name: Sainsbury, Sarah
last_name: Sainsbury
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Patrick
full_name: Cramer, Patrick
last_name: Cramer
citation:
ama: Sainsbury S, Bernecky C, Cramer P. Structural basis of transcription initiation
by RNA polymerase II. Nature Reviews Molecular Cell Biology. 2015;16(3):129-143.
doi:10.1038/nrm3952
apa: Sainsbury, S., Bernecky, C., & Cramer, P. (2015). Structural basis of transcription
initiation by RNA polymerase II. Nature Reviews Molecular Cell Biology.
Nature Publishing Group. https://doi.org/10.1038/nrm3952
chicago: Sainsbury, Sarah, Carrie Bernecky, and Patrick Cramer. “Structural Basis
of Transcription Initiation by RNA Polymerase II.” Nature Reviews Molecular
Cell Biology. Nature Publishing Group, 2015. https://doi.org/10.1038/nrm3952.
ieee: S. Sainsbury, C. Bernecky, and P. Cramer, “Structural basis of transcription
initiation by RNA polymerase II,” Nature Reviews Molecular Cell Biology,
vol. 16, no. 3. Nature Publishing Group, pp. 129–143, 2015.
ista: Sainsbury S, Bernecky C, Cramer P. 2015. Structural basis of transcription
initiation by RNA polymerase II. Nature Reviews Molecular Cell Biology. 16(3),
129–143.
mla: Sainsbury, Sarah, et al. “Structural Basis of Transcription Initiation by RNA
Polymerase II.” Nature Reviews Molecular Cell Biology, vol. 16, no. 3,
Nature Publishing Group, 2015, pp. 129–43, doi:10.1038/nrm3952.
short: S. Sainsbury, C. Bernecky, P. Cramer, Nature Reviews Molecular Cell Biology
16 (2015) 129–143.
date_created: 2018-12-11T11:47:23Z
date_published: 2015-03-26T00:00:00Z
date_updated: 2021-01-12T08:05:16Z
day: '26'
doi: 10.1038/nrm3952
extern: '1'
intvolume: ' 16'
issue: '3'
language:
- iso: eng
month: '03'
oa_version: None
page: 129 - 143
publication: Nature Reviews Molecular Cell Biology
publication_status: published
publisher: Nature Publishing Group
publist_id: '7206'
status: public
title: Structural basis of transcription initiation by RNA polymerase II
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 16
year: '2015'
...
---
_id: '595'
article_processing_charge: No
author:
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Patrick
full_name: Cramer, Patrick
last_name: Cramer
citation:
ama: 'Bernecky C, Cramer P. Struggling to let go: A non-coding RNA directs its own
extension and destruction. EMBO Journal. 2013;32(6):771-772. doi:10.1038/emboj.2013.36'
apa: 'Bernecky, C., & Cramer, P. (2013). Struggling to let go: A non-coding
RNA directs its own extension and destruction. EMBO Journal. Wiley-Blackwell.
https://doi.org/10.1038/emboj.2013.36'
chicago: 'Bernecky, Carrie, and Patrick Cramer. “Struggling to Let Go: A Non-Coding
RNA Directs Its Own Extension and Destruction.” EMBO Journal. Wiley-Blackwell,
2013. https://doi.org/10.1038/emboj.2013.36.'
ieee: 'C. Bernecky and P. Cramer, “Struggling to let go: A non-coding RNA directs
its own extension and destruction,” EMBO Journal, vol. 32, no. 6. Wiley-Blackwell,
pp. 771–772, 2013.'
ista: 'Bernecky C, Cramer P. 2013. Struggling to let go: A non-coding RNA directs
its own extension and destruction. EMBO Journal. 32(6), 771–772.'
mla: 'Bernecky, Carrie, and Patrick Cramer. “Struggling to Let Go: A Non-Coding
RNA Directs Its Own Extension and Destruction.” EMBO Journal, vol. 32,
no. 6, Wiley-Blackwell, 2013, pp. 771–72, doi:10.1038/emboj.2013.36.'
short: C. Bernecky, P. Cramer, EMBO Journal 32 (2013) 771–772.
date_created: 2018-12-11T11:47:23Z
date_published: 2013-03-20T00:00:00Z
date_updated: 2021-01-12T08:05:20Z
day: '20'
doi: 10.1038/emboj.2013.36
extern: '1'
intvolume: ' 32'
issue: '6'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3604726/
month: '03'
oa: 1
oa_version: None
page: 771 - 772
publication: EMBO Journal
publication_status: published
publisher: Wiley-Blackwell
publist_id: '7207'
status: public
title: 'Struggling to let go: A non-coding RNA directs its own extension and destruction'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 32
year: '2013'
...
---
_id: '596'
abstract:
- lang: eng
text: The human Mediator complex controls RNA polymerase II (pol II) function in
ways that remain incompletely understood. Activator-Mediator binding alters Mediator
structure, and these activator-induced structural shifts appear to play key roles
in regulating transcription. A recent cryo-electron microscopy (EM) analysis revealed
that pol II adopted a stable orientation within a Mediator-pol II-TFIIF assembly
in which Mediator was bound to the activation domain of viral protein 16 (VP16).
Whereas TFIIF was shown to be important for orienting pol II within this assembly,
the potential role of the activator was not assessed. To determine how activator
binding might affect pol II orientation, we isolated human Mediator-pol II-TFIIF
complexes in which Mediator was not bound to an activator. Cryo-EM analysis of
this assembly, coupled with pol II crystal structure docking, revealed that pol
II binds Mediator at the same general location; however, in contrast to VP16-bound
Mediator, pol II does not appear to stably orient in the absence of an activator.
Variability in pol II orientation might be important mechanistically, perhaps
to enable sense and antisense transcription at human promoters. Because Mediator
interacts extensively with pol II, these results suggest that Mediator structural
shifts induced by activator binding help stably orient pol II prior to transcription
initiation.
article_processing_charge: No
author:
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Dylan
full_name: Taatjes, Dylan
last_name: Taatjes
citation:
ama: Bernecky C, Taatjes D. Activator-mediator binding stabilizes RNA polymerase
II orientation within the human mediator-RNA polymerase II-TFIIF assembly. Journal
of Molecular Biology. 2012;417(5):387-394. doi:10.1016/j.jmb.2012.02.014
apa: Bernecky, C., & Taatjes, D. (2012). Activator-mediator binding stabilizes
RNA polymerase II orientation within the human mediator-RNA polymerase II-TFIIF
assembly. Journal of Molecular Biology. Elsevier. https://doi.org/10.1016/j.jmb.2012.02.014
chicago: Bernecky, Carrie, and Dylan Taatjes. “Activator-Mediator Binding Stabilizes
RNA Polymerase II Orientation within the Human Mediator-RNA Polymerase II-TFIIF
Assembly.” Journal of Molecular Biology. Elsevier, 2012. https://doi.org/10.1016/j.jmb.2012.02.014.
ieee: C. Bernecky and D. Taatjes, “Activator-mediator binding stabilizes RNA polymerase
II orientation within the human mediator-RNA polymerase II-TFIIF assembly,” Journal
of Molecular Biology, vol. 417, no. 5. Elsevier, pp. 387–394, 2012.
ista: Bernecky C, Taatjes D. 2012. Activator-mediator binding stabilizes RNA polymerase
II orientation within the human mediator-RNA polymerase II-TFIIF assembly. Journal
of Molecular Biology. 417(5), 387–394.
mla: Bernecky, Carrie, and Dylan Taatjes. “Activator-Mediator Binding Stabilizes
RNA Polymerase II Orientation within the Human Mediator-RNA Polymerase II-TFIIF
Assembly.” Journal of Molecular Biology, vol. 417, no. 5, Elsevier, 2012,
pp. 387–94, doi:10.1016/j.jmb.2012.02.014.
short: C. Bernecky, D. Taatjes, Journal of Molecular Biology 417 (2012) 387–394.
date_created: 2018-12-11T11:47:24Z
date_published: 2012-04-13T00:00:00Z
date_updated: 2021-01-12T08:05:21Z
day: '13'
doi: 10.1016/j.jmb.2012.02.014
extern: '1'
intvolume: ' 417'
issue: '5'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4582759/
month: '04'
oa: 1
oa_version: None
page: 387 - 394
publication: Journal of Molecular Biology
publication_status: published
publisher: Elsevier
publist_id: '7208'
status: public
title: Activator-mediator binding stabilizes RNA polymerase II orientation within
the human mediator-RNA polymerase II-TFIIF assembly
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 417
year: '2012'
...
---
_id: '597'
abstract:
- lang: eng
text: The macromolecular assembly required to initiate transcription of protein-coding
genes, known as the Pre-Initiation Complex (PIC), consists of multiple protein
complexes and is approximately 3.5 MDa in size. At the heart of this assembly
is the Mediator complex, which helps regulate PIC activity and interacts with
the RNA polymerase II (pol II) enzyme. The structure of the human Mediator-pol
II interface is not well-characterized, whereas attempts to structurally define
the Mediator-pol II interaction in yeast have relied on incomplete assemblies
of Mediator and/or pol II and have yielded inconsistent interpretations. We have
assembled the complete, 1.9 MDa human Mediator-pol II-TFIIF complex from purified
components and have characterized its structural organization using cryo-electron
microscopy and single-particle reconstruction techniques. The orientation of pol
II within this assembly was determined by crystal structure docking and further
validated with projection matching experiments, allowing the structural organization
of the entire human PIC to be envisioned. Significantly, pol II orientation within
the Mediator-pol II-TFIIF assembly can be reconciled with past studies that determined
the location of other PIC components relative to pol II itself. Pol II surfaces
required for interacting with TFIIB, TFIIE, and promoter DNA (i.e., the pol II
cleft) are exposed within the Mediator-pol II-TFIIF structure; RNA exit is unhindered
along the RPB4/7 subunits; upstream and downstream DNA is accessible for binding
additional factors; and no major structural re-organization is necessary to accommodate
the large, multi-subunit TFIIH or TFIID complexes. The data also reveal how pol
II binding excludes Mediator-CDK8 subcomplex interactions and provide a structural
basis for Mediator-dependent control of PIC assembly and function. Finally, parallel
structural analysis of Mediator-pol II complexes lacking TFIIF reveal that TFIIF
plays a key role in stabilizing pol II orientation within the assembly.
article_processing_charge: No
author:
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Patricia
full_name: Grob, Patricia
last_name: Grob
- first_name: Christopher
full_name: Ebmeier, Christopher
last_name: Ebmeier
- first_name: Eva
full_name: Nogales, Eva
last_name: Nogales
- first_name: Dylan
full_name: Taatjes, Dylan
last_name: Taatjes
citation:
ama: Bernecky C, Grob P, Ebmeier C, Nogales E, Taatjes D. Molecular architecture
of the human Mediator-RNA polymerase II-TFIIF assembly. PLoS Biology. 2011;9(3).
doi:10.1371/journal.pbio.1000603
apa: Bernecky, C., Grob, P., Ebmeier, C., Nogales, E., & Taatjes, D. (2011).
Molecular architecture of the human Mediator-RNA polymerase II-TFIIF assembly.
PLoS Biology. Public Library of Science. https://doi.org/10.1371/journal.pbio.1000603
chicago: Bernecky, Carrie, Patricia Grob, Christopher Ebmeier, Eva Nogales, and
Dylan Taatjes. “Molecular Architecture of the Human Mediator-RNA Polymerase II-TFIIF
Assembly.” PLoS Biology. Public Library of Science, 2011. https://doi.org/10.1371/journal.pbio.1000603.
ieee: C. Bernecky, P. Grob, C. Ebmeier, E. Nogales, and D. Taatjes, “Molecular architecture
of the human Mediator-RNA polymerase II-TFIIF assembly,” PLoS Biology,
vol. 9, no. 3. Public Library of Science, 2011.
ista: Bernecky C, Grob P, Ebmeier C, Nogales E, Taatjes D. 2011. Molecular architecture
of the human Mediator-RNA polymerase II-TFIIF assembly. PLoS Biology. 9(3).
mla: Bernecky, Carrie, et al. “Molecular Architecture of the Human Mediator-RNA
Polymerase II-TFIIF Assembly.” PLoS Biology, vol. 9, no. 3, Public Library
of Science, 2011, doi:10.1371/journal.pbio.1000603.
short: C. Bernecky, P. Grob, C. Ebmeier, E. Nogales, D. Taatjes, PLoS Biology 9
(2011).
date_created: 2018-12-11T11:47:24Z
date_published: 2011-03-01T00:00:00Z
date_updated: 2021-01-12T08:05:25Z
day: '01'
doi: 10.1371/journal.pbio.1000603
extern: '1'
intvolume: ' 9'
issue: '3'
language:
- iso: eng
month: '03'
oa_version: None
publication: PLoS Biology
publication_status: published
publisher: Public Library of Science
publist_id: '7209'
status: public
title: Molecular architecture of the human Mediator-RNA polymerase II-TFIIF assembly
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 9
year: '2011'
...
---
_id: '598'
abstract:
- lang: eng
text: It is not well understood how the human Mediator complex, transcription factor
IIH and RNA polymerase II (Pol II) work together with activators to initiate transcription.
Activator binding alters Mediator structure, yet the functional consequences of
such structural shifts remain unknown. The p53 C terminus and its activation domain
interact with different Mediator subunits, and we find that each interaction differentially
affects Mediator structure; strikingly, distinct p53-Mediator structures differentially
affect Pol II activity. Only the p53 activation domain induces the formation of
a large pocket domain at the Mediator-Pol II interaction site, and this correlates
with activation of stalled Pol II to a productively elongating state. Moreover,
we define a Mediator requirement for TFIIH-dependent Pol II C-terminal domain
phosphorylation and identify substantial differences in Pol II C-terminal domain
processing that correspond to distinct p53-Mediator structural states. Our results
define a fundamental mechanism by which p53 activates transcription and suggest
that Mediator structural shifts trigger activation of stalled Pol II complexes.
article_processing_charge: No
author:
- first_name: Krista
full_name: Meyer, Krista
last_name: Meyer
- first_name: Shih
full_name: Lin, Shih
last_name: Lin
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Yuefeng
full_name: Gao, Yuefeng
last_name: Gao
- first_name: Dylan
full_name: Taatjes, Dylan
last_name: Taatjes
citation:
ama: Meyer K, Lin S, Bernecky C, Gao Y, Taatjes D. P53 activates transcription by
directing structural shifts in Mediator. Nature Structural and Molecular Biology.
2010;17(6):753-760. doi:10.1038/nsmb.1816
apa: Meyer, K., Lin, S., Bernecky, C., Gao, Y., & Taatjes, D. (2010). P53 activates
transcription by directing structural shifts in Mediator. Nature Structural
and Molecular Biology. Nature Publishing Group. https://doi.org/10.1038/nsmb.1816
chicago: Meyer, Krista, Shih Lin, Carrie Bernecky, Yuefeng Gao, and Dylan Taatjes.
“P53 Activates Transcription by Directing Structural Shifts in Mediator.” Nature
Structural and Molecular Biology. Nature Publishing Group, 2010. https://doi.org/10.1038/nsmb.1816.
ieee: K. Meyer, S. Lin, C. Bernecky, Y. Gao, and D. Taatjes, “P53 activates transcription
by directing structural shifts in Mediator,” Nature Structural and Molecular
Biology, vol. 17, no. 6. Nature Publishing Group, pp. 753–760, 2010.
ista: Meyer K, Lin S, Bernecky C, Gao Y, Taatjes D. 2010. P53 activates transcription
by directing structural shifts in Mediator. Nature Structural and Molecular Biology.
17(6), 753–760.
mla: Meyer, Krista, et al. “P53 Activates Transcription by Directing Structural
Shifts in Mediator.” Nature Structural and Molecular Biology, vol. 17,
no. 6, Nature Publishing Group, 2010, pp. 753–60, doi:10.1038/nsmb.1816.
short: K. Meyer, S. Lin, C. Bernecky, Y. Gao, D. Taatjes, Nature Structural and
Molecular Biology 17 (2010) 753–760.
date_created: 2018-12-11T11:47:24Z
date_published: 2010-06-01T00:00:00Z
date_updated: 2021-01-12T08:05:28Z
day: '01'
doi: 10.1038/nsmb.1816
extern: '1'
intvolume: ' 17'
issue: '6'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2932482/
month: '06'
oa: 1
oa_version: None
page: 753 - 760
publication: Nature Structural and Molecular Biology
publication_status: published
publisher: Nature Publishing Group
publist_id: '7210'
status: public
title: P53 activates transcription by directing structural shifts in Mediator
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 17
year: '2010'
...
---
_id: '599'
abstract:
- lang: eng
text: The human CDK8 subcomplex (CDK8, cyclin C, Med12, and Med13) negatively regulates
transcription in ways not completely defined; past studies suggested CDK8 kinase
activity was required for its repressive function. Using a reconstituted transcription
system together with recombinant or endogenous CDK8 subcomplexes, we demonstrate
that, in fact, Med12 and Med13 are critical for subcomplex-dependent repression,
whereas CDK8 kinase activity is not. A hallmark of activated transcription is
efficient reinitiation from promoter-bound scaffold complexes that recruit a series
of pol II enzymes to the gene. Notably, the CDK8 submodule strongly represses
even reinitiation events, suggesting a means to fine tune transcript levels. Structural
and biochemical studies confirm the CDK8 submodule binds the Mediator leg/tail
domain via the Med13 subunit, and this submodule-Mediator association precludes
pol II recruitment. Collectively, these results reveal the CDK8 subcomplex functions
as a simple switch that controls the Mediator-pol II interaction to help regulate
transcription initiation and reinitiation events. As Mediator is generally required
for expression of protein-coding genes, this may reflect a common mechanism by
which activated transcription is shut down in human cells.
article_processing_charge: No
author:
- first_name: Matthew
full_name: Knuesel, Matthew
last_name: Knuesel
- first_name: Krista
full_name: Meyer, Krista
last_name: Meyer
- first_name: Carrie A
full_name: Bernecky, Carrie A
id: 2CB9DFE2-F248-11E8-B48F-1D18A9856A87
last_name: Bernecky
orcid: 0000-0003-0893-7036
- first_name: Dylan
full_name: Taatjes, Dylan
last_name: Taatjes
citation:
ama: Knuesel M, Meyer K, Bernecky C, Taatjes D. The human CDK8 subcomplex is a molecular
switch that controls Mediator coactivator function. Genes and Development.
2009;23(4):439-451. doi:10.1101/gad.1767009
apa: Knuesel, M., Meyer, K., Bernecky, C., & Taatjes, D. (2009). The human CDK8
subcomplex is a molecular switch that controls Mediator coactivator function.
Genes and Development. Cold Spring Harbor Laboratory Press. https://doi.org/10.1101/gad.1767009
chicago: Knuesel, Matthew, Krista Meyer, Carrie Bernecky, and Dylan Taatjes. “The
Human CDK8 Subcomplex Is a Molecular Switch That Controls Mediator Coactivator
Function.” Genes and Development. Cold Spring Harbor Laboratory Press,
2009. https://doi.org/10.1101/gad.1767009.
ieee: M. Knuesel, K. Meyer, C. Bernecky, and D. Taatjes, “The human CDK8 subcomplex
is a molecular switch that controls Mediator coactivator function,” Genes and
Development, vol. 23, no. 4. Cold Spring Harbor Laboratory Press, pp. 439–451,
2009.
ista: Knuesel M, Meyer K, Bernecky C, Taatjes D. 2009. The human CDK8 subcomplex
is a molecular switch that controls Mediator coactivator function. Genes and Development.
23(4), 439–451.
mla: Knuesel, Matthew, et al. “The Human CDK8 Subcomplex Is a Molecular Switch That
Controls Mediator Coactivator Function.” Genes and Development, vol. 23,
no. 4, Cold Spring Harbor Laboratory Press, 2009, pp. 439–51, doi:10.1101/gad.1767009.
short: M. Knuesel, K. Meyer, C. Bernecky, D. Taatjes, Genes and Development 23 (2009)
439–451.
date_created: 2018-12-11T11:47:25Z
date_published: 2009-02-15T00:00:00Z
date_updated: 2021-01-12T08:05:32Z
day: '15'
doi: 10.1101/gad.1767009
extern: '1'
intvolume: ' 23'
issue: '4'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2648653/
month: '02'
oa: 1
oa_version: None
page: 439 - 451
publication: Genes and Development
publication_status: published
publisher: Cold Spring Harbor Laboratory Press
publist_id: '7211'
status: public
title: The human CDK8 subcomplex is a molecular switch that controls Mediator coactivator
function
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 23
year: '2009'
...