---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
_id: '21509'
abstract:
- lang: eng
text: Chromatin remodeling complexes mobilize nucleosomes and promote transcription
factor (TF) binding. Using ensemble and single-molecule assays combined with cryo-electron
microscopy (cryo-EM), we studied the interaction between pioneer TFs OCT4–SOX2
and the human BRG1/BRM-associated factor (BAF) complex on nucleosomes. BAF engages
TF-bound substrates in two orientations, placing OCT4–SOX2 at either the remodeler
ENTRY or EXIT site. At the ENTRY site, OCT4–SOX2 initially coexists with BAF without
structural interference. However, continued DNA translocation is expected to cause
collisions with bound TFs, which can trigger remodeling direction reversals or
may induce TF dissociation. To accommodate TFs at the EXIT site, BAF undergoes
structural rearrangements, and ensemble assays reveal a nucleosome subpopulation
translocating away from TF-binding sites. Moreover, single-molecule experiments
show that nucleosome-bound BAF frequently changes remodeling direction, and we
identify an ADP-bound remodeler conformation as a potential intermediate. Together,
these findings reveal key aspects of the conformational dynamics and remodeling
outcomes underlying BAF processing of TF-bound nucleosomes.
acknowledgement: We thank D. Hess, V. Iesmantavicius, and J. Seebacher (FMI Proteomics
and Protein Analysis Facility) for mass spectrometry support; S. Smallwood, K. Shimada,
D. Klein, and M. Schütz-Stoffregen for technical assistance; J. Côté and C. Lachance
for critical discussions; and members of the Thomä lab for helpful feedback. Support
for this work was provided to N.H.T. by the European Research Council under the
European Union’s Horizon 2020 research program (NucEM, no. 884331), the Novartis
Research Foundation, the Swiss National Science Foundation (SNF 31003A_179541, 310030_214852,
and Sinergia CRSII5_186230), and the Swiss Cancer Research (KFS-4980-02-2020 and
KFS-5933-08-2023). S.D. was supported by the European Research Council (DONUTS,
no. 101092623), the Knut and Alice Wallenberg Foundation (2024.0012), the Cancerfonden
(25 4453 Pj), and the Swedish Research Council (VR 03255). A.K.M. was supported
by a Human Frontier Science Program Long-Term Fellowship, and L.V. was supported
by an EMBO fellowship (ALTF 549-2021).
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Joscha
full_name: Weiss, Joscha
last_name: Weiss
- first_name: Luca
full_name: Vecchia, Luca
last_name: Vecchia
- first_name: David
full_name: Domjan, David
last_name: Domjan
- first_name: Simone
full_name: Cavadini, Simone
last_name: Cavadini
- first_name: Anton
full_name: Sabantsev, Anton
last_name: Sabantsev
- first_name: Georg
full_name: Kempf, Georg
last_name: Kempf
- first_name: Ganesh R.
full_name: Pathare, Ganesh R.
last_name: Pathare
- first_name: Klaus
full_name: Brackmann, Klaus
last_name: Brackmann
- first_name: Alicia
full_name: Michael, Alicia
id: 6437c950-2a03-11ee-914d-d6476dd7b75c
last_name: Michael
orcid: 0000-0002-6080-839X
- first_name: Lukas
full_name: Kater, Lukas
last_name: Kater
- first_name: Eric
full_name: Hietter-Pfeiffer, Eric
last_name: Hietter-Pfeiffer
- first_name: Mina
full_name: Haddawi, Mina
last_name: Haddawi
- first_name: Urja P.
full_name: Kuber, Urja P.
last_name: Kuber
- first_name: Sandra
full_name: Mühlhäusser, Sandra
last_name: Mühlhäusser
- first_name: Ralph S.
full_name: Grand, Ralph S.
last_name: Grand
- first_name: Michael B.
full_name: Stadler, Michael B.
last_name: Stadler
- first_name: Sebastian
full_name: Deindl, Sebastian
last_name: Deindl
- first_name: Nicolas H.
full_name: Thomä, Nicolas H.
last_name: Thomä
citation:
ama: Weiss J, Vecchia L, Domjan D, et al. The human BAF chromatin remodeler processes
nucleosomes bound by pioneer transcription factors OCT4–SOX2. Molecular Cell.
2026;86(4):625-639.e8. doi:10.1016/j.molcel.2026.01.021
apa: Weiss, J., Vecchia, L., Domjan, D., Cavadini, S., Sabantsev, A., Kempf, G.,
… Thomä, N. H. (2026). The human BAF chromatin remodeler processes nucleosomes
bound by pioneer transcription factors OCT4–SOX2. Molecular Cell. Elsevier.
https://doi.org/10.1016/j.molcel.2026.01.021
chicago: Weiss, Joscha, Luca Vecchia, David Domjan, Simone Cavadini, Anton Sabantsev,
Georg Kempf, Ganesh R. Pathare, et al. “The Human BAF Chromatin Remodeler Processes
Nucleosomes Bound by Pioneer Transcription Factors OCT4–SOX2.” Molecular Cell.
Elsevier, 2026. https://doi.org/10.1016/j.molcel.2026.01.021.
ieee: J. Weiss et al., “The human BAF chromatin remodeler processes nucleosomes
bound by pioneer transcription factors OCT4–SOX2,” Molecular Cell, vol.
86, no. 4. Elsevier, p. 625–639.e8, 2026.
ista: Weiss J, Vecchia L, Domjan D, Cavadini S, Sabantsev A, Kempf G, Pathare GR,
Brackmann K, Michael AK, Kater L, Hietter-Pfeiffer E, Haddawi M, Kuber UP, Mühlhäusser
S, Grand RS, Stadler MB, Deindl S, Thomä NH. 2026. The human BAF chromatin remodeler
processes nucleosomes bound by pioneer transcription factors OCT4–SOX2. Molecular
Cell. 86(4), 625–639.e8.
mla: Weiss, Joscha, et al. “The Human BAF Chromatin Remodeler Processes Nucleosomes
Bound by Pioneer Transcription Factors OCT4–SOX2.” Molecular Cell, vol.
86, no. 4, Elsevier, 2026, p. 625–639.e8, doi:10.1016/j.molcel.2026.01.021.
short: J. Weiss, L. Vecchia, D. Domjan, S. Cavadini, A. Sabantsev, G. Kempf, G.R.
Pathare, K. Brackmann, A.K. Michael, L. Kater, E. Hietter-Pfeiffer, M. Haddawi,
U.P. Kuber, S. Mühlhäusser, R.S. Grand, M.B. Stadler, S. Deindl, N.H. Thomä, Molecular
Cell 86 (2026) 625–639.e8.
date_created: 2026-03-30T11:58:48Z
date_published: 2026-02-19T00:00:00Z
date_updated: 2026-03-30T12:09:08Z
day: '19'
ddc:
- '570'
department:
- _id: AlMi
doi: 10.1016/j.molcel.2026.01.021
external_id:
pmid:
- '41679301'
file:
- access_level: open_access
checksum: e16a7315b64a706184b177ea1621523c
content_type: application/pdf
creator: dernst
date_created: 2026-03-30T12:04:38Z
date_updated: 2026-03-30T12:04:38Z
file_id: '21510'
file_name: 2026_MolecularCell_Weiss.pdf
file_size: 9786677
relation: main_file
success: 1
file_date_updated: 2026-03-30T12:04:38Z
has_accepted_license: '1'
intvolume: ' 86'
issue: '4'
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
page: 625-639.e8
pmid: 1
publication: Molecular Cell
publication_identifier:
issn:
- 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: The human BAF chromatin remodeler processes nucleosomes bound by pioneer transcription
factors OCT4–SOX2
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: 86
year: '2026'
...
---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
_id: '20374'
abstract:
- lang: eng
text: Pioneer transcription factors (TFs) engage chromatinized DNA motifs. However,
it is unclear how the resultant TF-nucleosome complexes are decoded by co-factors.
In humans, the TF p53 regulates cell-cycle progression, apoptosis, and the DNA
damage response, with a large fraction of p53-bound sites residing in nucleosome-harboring
inaccessible chromatin. We examined the interaction of chromatin-bound p53 with
co-factors belonging to the ubiquitin proteasome system (UPS). At two distinct
motif locations on the nucleosome (super-helical location [SHL]−5.7 and SHL+5.9),
the E3 ubiquitin ligase E6-E6AP was unable to bind nucleosome-engaged p53. The
deubiquitinase USP7, on the other hand, readily engages nucleosome-bound p53 in
vitro and in cells. A corresponding cryo-electron microscopy (cryo-EM) structure
shows USP7 engaged with p53 and nucleosomes. Our work illustrates how chromatin
imposes a co-factor-selective barrier for p53 interactors, whereby flexibly tethered
interaction domains of co-factors and TFs govern compatibility between co-factors,
TFs, and chromatin.
acknowledgement: We thank M. Schütz for laboratory management, organization, and assistance
with manuscript editing. We are grateful to all Thomä and Schübeler lab members.
We thank Ulrich Hassiepen from Novartis for his support and insightful discussions
on the kinetic analysis. This work was supported by funding from the European Research
Council (ERC), under the European Union’s H2020 research program (NucEM, grant no.
884331); the Swiss National Science Foundation (SNF, grant no. 310030_301206 and
310030_214852); Krebsforschung (KFS, grant no. KFS-5933-08-2023); Novartis Research
Foundation (to N.H.T.); the Novartis Freenovation (grant no. FN23-0000000514 to
C.R.S.); the National Health and Medical Research Council CJ Martin Fellowship (APP1148380);
the EU Horizon 2020 Research and Innovation Program under the Marie Sklodowska-Curie
grant (grant no. 748760); the South Australian immunoGENomics Cancer Institute grant
funding from the Australian Government; and the Sylvia and Charles Viertel Charitable
Foundation Senior Medical Research Fellowship (to L.I.).
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Deyasini
full_name: Chakraborty, Deyasini
last_name: Chakraborty
- first_name: Colby R.
full_name: Sandate, Colby R.
last_name: Sandate
- first_name: Luke
full_name: Isbel, Luke
last_name: Isbel
- first_name: Georg
full_name: Kempf, Georg
last_name: Kempf
- first_name: Joscha
full_name: Weiss, Joscha
last_name: Weiss
- first_name: Simone
full_name: Cavadini, Simone
last_name: Cavadini
- first_name: Lukas
full_name: Kater, Lukas
last_name: Kater
- first_name: Jan
full_name: Seebacher, Jan
last_name: Seebacher
- first_name: Zuzanna
full_name: Kozicka, Zuzanna
last_name: Kozicka
- first_name: Lisa
full_name: Stoos, Lisa
last_name: Stoos
- first_name: Ralph S.
full_name: Grand, Ralph S.
last_name: Grand
- first_name: Dirk
full_name: Schübeler, Dirk
last_name: Schübeler
- first_name: Alicia
full_name: Michael, Alicia
id: 6437c950-2a03-11ee-914d-d6476dd7b75c
last_name: Michael
orcid: 0000-0002-6080-839X
- first_name: Nicolas H.
full_name: Thomä, Nicolas H.
last_name: Thomä
citation:
ama: Chakraborty D, Sandate CR, Isbel L, et al. Nucleosomes specify co-factor access
to p53. Molecular Cell. 2025;85(15):2919-2936.e12. doi:10.1016/j.molcel.2025.06.027
apa: Chakraborty, D., Sandate, C. R., Isbel, L., Kempf, G., Weiss, J., Cavadini,
S., … Thomä, N. H. (2025). Nucleosomes specify co-factor access to p53. Molecular
Cell. Elsevier. https://doi.org/10.1016/j.molcel.2025.06.027
chicago: Chakraborty, Deyasini, Colby R. Sandate, Luke Isbel, Georg Kempf, Joscha
Weiss, Simone Cavadini, Lukas Kater, et al. “Nucleosomes Specify Co-Factor Access
to P53.” Molecular Cell. Elsevier, 2025. https://doi.org/10.1016/j.molcel.2025.06.027.
ieee: D. Chakraborty et al., “Nucleosomes specify co-factor access to p53,”
Molecular Cell, vol. 85, no. 15. Elsevier, p. 2919–2936.e12, 2025.
ista: Chakraborty D, Sandate CR, Isbel L, Kempf G, Weiss J, Cavadini S, Kater L,
Seebacher J, Kozicka Z, Stoos L, Grand RS, Schübeler D, Michael AK, Thomä NH.
2025. Nucleosomes specify co-factor access to p53. Molecular Cell. 85(15), 2919–2936.e12.
mla: Chakraborty, Deyasini, et al. “Nucleosomes Specify Co-Factor Access to P53.”
Molecular Cell, vol. 85, no. 15, Elsevier, 2025, p. 2919–2936.e12, doi:10.1016/j.molcel.2025.06.027.
short: D. Chakraborty, C.R. Sandate, L. Isbel, G. Kempf, J. Weiss, S. Cavadini,
L. Kater, J. Seebacher, Z. Kozicka, L. Stoos, R.S. Grand, D. Schübeler, A.K. Michael,
N.H. Thomä, Molecular Cell 85 (2025) 2919–2936.e12.
date_created: 2025-09-23T08:56:13Z
date_published: 2025-08-07T00:00:00Z
date_updated: 2025-09-24T08:21:55Z
day: '07'
ddc:
- '570'
department:
- _id: AlMi
doi: 10.1016/j.molcel.2025.06.027
file:
- access_level: open_access
checksum: e60390ca629b350af3221d4718ca6534
content_type: application/pdf
creator: dernst
date_created: 2025-09-24T07:54:03Z
date_updated: 2025-09-24T07:54:03Z
file_id: '20386'
file_name: 2025_MolecularCell_Chakraborty.pdf
file_size: 41813494
relation: main_file
success: 1
file_date_updated: 2025-09-24T07:54:03Z
has_accepted_license: '1'
intvolume: ' 85'
issue: '15'
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
page: 2919-2936.e12
publication: Molecular Cell
publication_identifier:
issn:
- 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nucleosomes specify co-factor access to p53
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: 85
year: '2025'
...
---
OA_place: publisher
OA_type: hybrid
PlanS_conform: '1'
_id: '20935'
abstract:
- lang: eng
text: In situ cryo-electron tomography (cryo-ET) has emerged as the method of choice
to investigate the structures of biomolecules in their native context. However,
challenges remain for the efficient production and sharing of large-scale cryo-ET
datasets. Here, we combined cryogenic plasma-based focused ion beam (cryo-PFIB)
milling with recent advances in cryo-ET acquisition and processing to generate
a dataset of 1,829 annotated tomograms of the green alga Chlamydomonas reinhardtii,
which we provide as a community resource to drive method development and inspire
biological discovery. To assay data quality, we performed subtomogram averaging
of both soluble and membrane-bound complexes ranging in size from >3 MDa to ∼200
kDa, including 80S ribosomes, Rubisco, nucleosomes, microtubules, clathrin, photosystem
II, and mitochondrial ATP synthase. The majority of these density maps reached
sub-nanometer resolution, demonstrating the potential of this C. reinhardtii dataset
as well as the promise of modern cryo-ET workflows and open data sharing to empower
visual proteomics.
acknowledgement: Calculations were performed at the Max Planck Institute of Biochemistry
and the Raven Supercomputer of the Max Planck Computing and Data Facility (MPCDF)
in Garching, Germany; at the sciCORE (http://scicore.unibas.ch/) scientific computing
center at the University of Basel, Switzerland; and at Thermo Fisher Scientific,
in Eindhoven, the Netherlands. This work was supported by Thermo Fisher Scientific.
All lamella preparations and tilt-series collections used in this work were conducted
at Thermo Fisher R&D facilities in Brno and Eindhoven, utilizing Arctis and Krios
microscopes. This work was also supported by the ERC consolidator grant “cryOcean”
(fulfilled by the Swiss State Secretariat for Education, Research and Innovation,
M822.00045) as well as a Swiss Nanoscience Institute PhD school grant to B.D.E.
and P.V.d.S., an EMBO long-term postdoctoral fellowship (ALTF-383-2022) to G.T.,
an SNSF Postdoctoral Fellowship (project 210561) to F.W., a Boehringer Ingelheim
Fonds fellowship to L.L., and by the Max Planck Society to J.A.G.B. and J.M.P.
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Ron
full_name: Kelley, Ron
last_name: Kelley
- first_name: Sagar
full_name: Khavnekar, Sagar
last_name: Khavnekar
- first_name: Ricardo D.
full_name: Righetto, Ricardo D.
last_name: Righetto
- first_name: Jessica
full_name: Heebner, Jessica
last_name: Heebner
- first_name: Martin
full_name: Obr, Martin
id: 4741CA5A-F248-11E8-B48F-1D18A9856A87
last_name: Obr
orcid: 0000-0003-1756-6564
- first_name: Xianjun
full_name: Zhang, Xianjun
last_name: Zhang
- first_name: Saikat
full_name: Chakraborty, Saikat
last_name: Chakraborty
- first_name: Grigory
full_name: Tagiltsev, Grigory
last_name: Tagiltsev
- first_name: Alicia
full_name: Michael, Alicia
id: 6437c950-2a03-11ee-914d-d6476dd7b75c
last_name: Michael
orcid: 0000-0002-6080-839X
- first_name: Sofie
full_name: Van Dorst, Sofie
last_name: Van Dorst
- first_name: Florent
full_name: Waltz, Florent
last_name: Waltz
- first_name: Caitlyn L.
full_name: Mccafferty, Caitlyn L.
last_name: Mccafferty
- first_name: Lorenz
full_name: Lamm, Lorenz
last_name: Lamm
- first_name: Simon
full_name: Zufferey, Simon
last_name: Zufferey
- first_name: Philippe
full_name: Van Der Stappen, Philippe
last_name: Van Der Stappen
- first_name: Hugo
full_name: Van Den Hoek, Hugo
last_name: Van Den Hoek
- first_name: Wojciech
full_name: Wietrzynski, Wojciech
last_name: Wietrzynski
- first_name: Pavol
full_name: Harar, Pavol
id: e03d953a-6e8c-11ef-99e4-f0717d385cd5
last_name: Harar
orcid: 0000-0001-5206-1794
- first_name: William
full_name: Wan, William
last_name: Wan
- first_name: John A.G.
full_name: Briggs, John A.G.
last_name: Briggs
- first_name: Jürgen M.
full_name: Plitzko, Jürgen M.
last_name: Plitzko
- first_name: Benjamin D.
full_name: Engel, Benjamin D.
last_name: Engel
- first_name: Abhay
full_name: Kotecha, Abhay
last_name: Kotecha
citation:
ama: Kelley R, Khavnekar S, Righetto RD, et al. Toward community-driven visual proteomics
with large-scale cryo-electron tomography of Chlamydomonas reinhardtii. Molecular
Cell. doi:10.1016/j.molcel.2025.11.029
apa: Kelley, R., Khavnekar, S., Righetto, R. D., Heebner, J., Obr, M., Zhang, X.,
… Kotecha, A. (n.d.). Toward community-driven visual proteomics with large-scale
cryo-electron tomography of Chlamydomonas reinhardtii. Molecular Cell.
Elsevier. https://doi.org/10.1016/j.molcel.2025.11.029
chicago: Kelley, Ron, Sagar Khavnekar, Ricardo D. Righetto, Jessica Heebner, Martin
Obr, Xianjun Zhang, Saikat Chakraborty, et al. “Toward Community-Driven Visual
Proteomics with Large-Scale Cryo-Electron Tomography of Chlamydomonas Reinhardtii.”
Molecular Cell. Elsevier, n.d. https://doi.org/10.1016/j.molcel.2025.11.029.
ieee: R. Kelley et al., “Toward community-driven visual proteomics with large-scale
cryo-electron tomography of Chlamydomonas reinhardtii,” Molecular Cell.
Elsevier.
ista: Kelley R, Khavnekar S, Righetto RD, Heebner J, Obr M, Zhang X, Chakraborty
S, Tagiltsev G, Michael AK, Van Dorst S, Waltz F, Mccafferty CL, Lamm L, Zufferey
S, Van Der Stappen P, Van Den Hoek H, Wietrzynski W, Harar P, Wan W, Briggs JAG,
Plitzko JM, Engel BD, Kotecha A. Toward community-driven visual proteomics with
large-scale cryo-electron tomography of Chlamydomonas reinhardtii. Molecular Cell.
mla: Kelley, Ron, et al. “Toward Community-Driven Visual Proteomics with Large-Scale
Cryo-Electron Tomography of Chlamydomonas Reinhardtii.” Molecular Cell,
Elsevier, doi:10.1016/j.molcel.2025.11.029.
short: R. Kelley, S. Khavnekar, R.D. Righetto, J. Heebner, M. Obr, X. Zhang, S.
Chakraborty, G. Tagiltsev, A.K. Michael, S. Van Dorst, F. Waltz, C.L. Mccafferty,
L. Lamm, S. Zufferey, P. Van Der Stappen, H. Van Den Hoek, W. Wietrzynski, P.
Harar, W. Wan, J.A.G. Briggs, J.M. Plitzko, B.D. Engel, A. Kotecha, Molecular
Cell (n.d.).
date_created: 2026-01-04T23:01:36Z
date_published: 2025-12-19T00:00:00Z
date_updated: 2026-01-05T08:32:47Z
day: '19'
ddc:
- '570'
department:
- _id: AlMi
doi: 10.1016/j.molcel.2025.11.029
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.molcel.2025.11.029
month: '12'
oa: 1
oa_version: Published Version
publication: Molecular Cell
publication_identifier:
eissn:
- 1097-4164
issn:
- 1097-2765
publication_status: inpress
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Toward community-driven visual proteomics with large-scale cryo-electron tomography
of Chlamydomonas reinhardtii
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
year: '2025'
...
---
_id: '18072'
abstract:
- lang: eng
text: The individualization of chromosomes during early mitosis and their clustering
upon exit from cell division are two key transitions that ensure efficient segregation
of eukaryotic chromosomes. Both processes are regulated by the surfactant-like
protein Ki-67, but how Ki-67 achieves these diametric functions has remained unknown.
Here, we report that Ki-67 radically switches from a chromosome repellent to a
chromosome attractant during anaphase in human cells. We show that Ki-67 dephosphorylation
during mitotic exit and the simultaneous exposure of a conserved basic patch induce
the RNA-dependent formation of a liquid-like condensed phase on the chromosome
surface. Experiments and coarse-grained simulations support a model in which the
coalescence of chromosome surfaces, driven by co-condensation of Ki-67 and RNA,
promotes clustering of chromosomes. Our study reveals how the switch of Ki-67
from a surfactant to a liquid-like condensed phase can generate mechanical forces
during genome segregation that are required for re-establishing nuclear-cytoplasmic
compartmentalization after mitosis.
acknowledgement: We thank Daniel W. Gerlich for providing cell lines, the EMBL Advanced
Light Microscopy Facility (ALMF) for support, Christian H. Haering and Thomas Quail
for input on the manuscript, and Martina Dees for cloning several Ki-67 constructs.
This work was supported by the German Research Foundation (DFG project number 402723784)
and the Human Frontier Science Program (CDA00045/2019). A.H.-A. and A.B. have received
PhD fellowships from the Boehringer Ingelheim Fonds, V.S. and A.Š. were supported
by the European Research Council (ERC) under the European Union’s Horizon 2020 research
and innovation programme (grant no. 802960), and Y.H. was supported by a fellowship
from the EMBL interdisciplinary Postdoc (EIPOD) program (Marie Sklodowska-Curie
Actions, COFUND grant agreement 664726).
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Alberto
full_name: Hernandez-Armendariz, Alberto
last_name: Hernandez-Armendariz
- first_name: Valerio
full_name: Sorichetti, Valerio
id: ef8a92cb-c7b6-11ec-8bea-e1fd5847bc5b
last_name: Sorichetti
orcid: 0000-0002-9645-6576
- first_name: Yuki
full_name: Hayashi, Yuki
last_name: Hayashi
- first_name: Zuzana
full_name: Koskova, Zuzana
last_name: Koskova
- first_name: Andreas
full_name: Brunner, Andreas
last_name: Brunner
- first_name: Jan
full_name: Ellenberg, Jan
last_name: Ellenberg
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Sara
full_name: Cuylen-Haering, Sara
last_name: Cuylen-Haering
citation:
ama: Hernandez-Armendariz A, Sorichetti V, Hayashi Y, et al. A liquid-like coat
mediates chromosome clustering during mitotic exit. Molecular Cell. 2024;84(17):P3254-3270.E9.
doi:10.1016/j.molcel.2024.07.022
apa: Hernandez-Armendariz, A., Sorichetti, V., Hayashi, Y., Koskova, Z., Brunner,
A., Ellenberg, J., … Cuylen-Haering, S. (2024). A liquid-like coat mediates chromosome
clustering during mitotic exit. Molecular Cell. Cell Press. https://doi.org/10.1016/j.molcel.2024.07.022
chicago: Hernandez-Armendariz, Alberto, Valerio Sorichetti, Yuki Hayashi, Zuzana
Koskova, Andreas Brunner, Jan Ellenberg, Anđela Šarić, and Sara Cuylen-Haering.
“A Liquid-like Coat Mediates Chromosome Clustering during Mitotic Exit.” Molecular
Cell. Cell Press, 2024. https://doi.org/10.1016/j.molcel.2024.07.022.
ieee: A. Hernandez-Armendariz et al., “A liquid-like coat mediates chromosome
clustering during mitotic exit,” Molecular Cell, vol. 84, no. 17. Cell
Press, p. P3254–3270.E9, 2024.
ista: Hernandez-Armendariz A, Sorichetti V, Hayashi Y, Koskova Z, Brunner A, Ellenberg
J, Šarić A, Cuylen-Haering S. 2024. A liquid-like coat mediates chromosome clustering
during mitotic exit. Molecular Cell. 84(17), P3254–3270.E9.
mla: Hernandez-Armendariz, Alberto, et al. “A Liquid-like Coat Mediates Chromosome
Clustering during Mitotic Exit.” Molecular Cell, vol. 84, no. 17, Cell
Press, 2024, p. P3254–3270.E9, doi:10.1016/j.molcel.2024.07.022.
short: A. Hernandez-Armendariz, V. Sorichetti, Y. Hayashi, Z. Koskova, A. Brunner,
J. Ellenberg, A. Šarić, S. Cuylen-Haering, Molecular Cell 84 (2024) P3254–3270.E9.
date_created: 2024-09-15T22:01:41Z
date_published: 2024-09-05T00:00:00Z
date_updated: 2025-09-08T09:23:02Z
day: '05'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1016/j.molcel.2024.07.022
ec_funded: 1
external_id:
isi:
- '001309051100001'
pmid:
- '39153474'
file:
- access_level: open_access
checksum: 3f360e0287b8ec79fb2b8b02b5070360
content_type: application/pdf
creator: dernst
date_created: 2024-09-16T07:38:38Z
date_updated: 2024-09-16T07:38:38Z
file_id: '18075'
file_name: 2024_MolecularCell_HernandezArmendariz.pdf
file_size: 11654644
relation: main_file
success: 1
file_date_updated: 2024-09-16T07:38:38Z
has_accepted_license: '1'
intvolume: ' 84'
isi: 1
issue: '17'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
page: P3254-3270.E9
pmid: 1
project:
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
publication: Molecular Cell
publication_identifier:
eissn:
- 1097-4164
issn:
- 1097-2765
publication_status: published
publisher: Cell Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: A liquid-like coat mediates chromosome clustering during mitotic exit
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'
...
---
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:
- '001395711300001'
pmid:
- '39547223'
file:
- access_level: open_access
checksum: e051e2766b2d424983778f742cb7c5ed
content_type: application/pdf
creator: dernst
date_created: 2025-01-13T11:17:35Z
date_updated: 2025-01-13T11:17:35Z
file_id: '18844'
file_name: 2024_MolecularCell_Ramadhin.pdf
file_size: 25071994
relation: main_file
success: 1
file_date_updated: 2025-01-13T11:17:35Z
has_accepted_license: '1'
intvolume: ' 84'
isi: 1
issue: '24'
language:
- iso: eng
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: '15129'
abstract:
- lang: eng
text: Type I CRISPR-Cas systems employ multi-subunit Cascade effector complexes
to target foreign nucleic acids for destruction. Here, we present structures of
D. vulgaris type I-C Cascade at various stages of double-stranded (ds)DNA target
capture, revealing mechanisms that underpin PAM recognition and Cascade allosteric
activation. We uncover an interesting mechanism of non-target strand (NTS) DNA
stabilization via stacking interactions with the “belly” subunits, securing the
NTS in place. This “molecular seatbelt” mechanism facilitates efficient R-loop
formation and prevents dsDNA reannealing. Additionally, we provide structural
insights into how two anti-CRISPR (Acr) proteins utilize distinct strategies to
achieve a shared mechanism of type I-C Cascade inhibition by blocking PAM scanning.
These observations form a structural basis for directional R-loop formation and
reveal how different Acr proteins have converged upon common molecular mechanisms
to efficiently shut down CRISPR immunity.
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Roisin E.
full_name: O’Brien, Roisin E.
last_name: O’Brien
- first_name: Jack Peter Kelly
full_name: Bravo, Jack Peter Kelly
id: 96aecfa5-8931-11ee-af30-aa6a5d6eee0e
last_name: Bravo
orcid: 0000-0003-0456-0753
- first_name: Delisa
full_name: Ramos, Delisa
last_name: Ramos
- first_name: Grace N.
full_name: Hibshman, Grace N.
last_name: Hibshman
- first_name: Jacquelyn T.
full_name: Wright, Jacquelyn T.
last_name: Wright
- first_name: David W.
full_name: Taylor, David W.
last_name: Taylor
citation:
ama: O’Brien RE, Bravo JPK, Ramos D, Hibshman GN, Wright JT, Taylor DW. Structural
snapshots of R-loop formation by a type I-C CRISPR Cascade. Molecular Cell.
2023;83(5):746-758.e5. doi:10.1016/j.molcel.2023.01.024
apa: O’Brien, R. E., Bravo, J. P. K., Ramos, D., Hibshman, G. N., Wright, J. T.,
& Taylor, D. W. (2023). Structural snapshots of R-loop formation by a type
I-C CRISPR Cascade. Molecular Cell. Elsevier. https://doi.org/10.1016/j.molcel.2023.01.024
chicago: O’Brien, Roisin E., Jack Peter Kelly Bravo, Delisa Ramos, Grace N. Hibshman,
Jacquelyn T. Wright, and David W. Taylor. “Structural Snapshots of R-Loop Formation
by a Type I-C CRISPR Cascade.” Molecular Cell. Elsevier, 2023. https://doi.org/10.1016/j.molcel.2023.01.024.
ieee: R. E. O’Brien, J. P. K. Bravo, D. Ramos, G. N. Hibshman, J. T. Wright, and
D. W. Taylor, “Structural snapshots of R-loop formation by a type I-C CRISPR Cascade,”
Molecular Cell, vol. 83, no. 5. Elsevier, p. 746–758.e5, 2023.
ista: O’Brien RE, Bravo JPK, Ramos D, Hibshman GN, Wright JT, Taylor DW. 2023. Structural
snapshots of R-loop formation by a type I-C CRISPR Cascade. Molecular Cell. 83(5),
746–758.e5.
mla: O’Brien, Roisin E., et al. “Structural Snapshots of R-Loop Formation by a Type
I-C CRISPR Cascade.” Molecular Cell, vol. 83, no. 5, Elsevier, 2023, p.
746–758.e5, doi:10.1016/j.molcel.2023.01.024.
short: R.E. O’Brien, J.P.K. Bravo, D. Ramos, G.N. Hibshman, J.T. Wright, D.W. Taylor,
Molecular Cell 83 (2023) 746–758.e5.
date_created: 2024-03-20T10:40:56Z
date_published: 2023-03-02T00:00:00Z
date_updated: 2024-06-04T06:33:54Z
day: '02'
doi: 10.1016/j.molcel.2023.01.024
extern: '1'
external_id:
pmid:
- '36805026'
intvolume: ' 83'
issue: '5'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.molcel.2023.01.024
month: '03'
oa: 1
oa_version: Published Version
page: 746-758.e5
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 snapshots of R-loop formation by a type I-C CRISPR Cascade
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 83
year: '2023'
...
---
_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: '15140'
abstract:
- lang: eng
text: Remdesivir is a nucleoside analog approved by the US FDA for treatment of
COVID-19. Here, we present a 3.9-Å-resolution cryo-EM reconstruction of a remdesivir-stalled
RNA-dependent RNA polymerase complex, revealing full incorporation of 3 copies
of remdesivir monophosphate (RMP) and a partially incorporated fourth RMP in the
active site. The structure reveals that RMP blocks RNA translocation after incorporation
of 3 bases following RMP, resulting in delayed chain termination, which can guide
the rational design of improved antiviral drugs.
article_processing_charge: No
article_type: original
author:
- first_name: Jack Peter Kelly
full_name: Bravo, Jack Peter Kelly
id: 96aecfa5-8931-11ee-af30-aa6a5d6eee0e
last_name: Bravo
orcid: 0000-0003-0456-0753
- first_name: Tyler L.
full_name: Dangerfield, Tyler L.
last_name: Dangerfield
- first_name: David W.
full_name: Taylor, David W.
last_name: Taylor
- first_name: Kenneth A.
full_name: Johnson, Kenneth A.
last_name: Johnson
citation:
ama: Bravo JPK, Dangerfield TL, Taylor DW, Johnson KA. Remdesivir is a delayed translocation
inhibitor of SARS-CoV-2 replication. Molecular Cell. 2021;81(7):1548-1552.e4.
doi:10.1016/j.molcel.2021.01.035
apa: Bravo, J. P. K., Dangerfield, T. L., Taylor, D. W., & Johnson, K. A. (2021).
Remdesivir is a delayed translocation inhibitor of SARS-CoV-2 replication. Molecular
Cell. Elsevier. https://doi.org/10.1016/j.molcel.2021.01.035
chicago: Bravo, Jack Peter Kelly, Tyler L. Dangerfield, David W. Taylor, and Kenneth
A. Johnson. “Remdesivir Is a Delayed Translocation Inhibitor of SARS-CoV-2 Replication.”
Molecular Cell. Elsevier, 2021. https://doi.org/10.1016/j.molcel.2021.01.035.
ieee: J. P. K. Bravo, T. L. Dangerfield, D. W. Taylor, and K. A. Johnson, “Remdesivir
is a delayed translocation inhibitor of SARS-CoV-2 replication,” Molecular
Cell, vol. 81, no. 7. Elsevier, p. 1548–1552.e4, 2021.
ista: Bravo JPK, Dangerfield TL, Taylor DW, Johnson KA. 2021. Remdesivir is a delayed
translocation inhibitor of SARS-CoV-2 replication. Molecular Cell. 81(7), 1548–1552.e4.
mla: Bravo, Jack Peter Kelly, et al. “Remdesivir Is a Delayed Translocation Inhibitor
of SARS-CoV-2 Replication.” Molecular Cell, vol. 81, no. 7, Elsevier, 2021,
p. 1548–1552.e4, doi:10.1016/j.molcel.2021.01.035.
short: J.P.K. Bravo, T.L. Dangerfield, D.W. Taylor, K.A. Johnson, Molecular Cell
81 (2021) 1548–1552.e4.
date_created: 2024-03-20T10:42:53Z
date_published: 2021-04-01T00:00:00Z
date_updated: 2024-06-04T06:00:56Z
day: '01'
doi: 10.1016/j.molcel.2021.01.035
extern: '1'
external_id:
pmid:
- '33631104'
intvolume: ' 81'
issue: '7'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: 'https://doi.org/10.1101/2020.12.14.422718 '
month: '04'
oa: 1
oa_version: Preprint
page: 1548-1552.e4
pmid: 1
publication: Molecular Cell
publication_identifier:
issn:
- 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Remdesivir is a delayed translocation inhibitor of SARS-CoV-2 replication
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 81
year: '2021'
...
---
OA_place: publisher
OA_type: hybrid
_id: '9526'
abstract:
- lang: eng
text: DNA methylation and histone H1 mediate transcriptional silencing of genes
and transposable elements, but how they interact is unclear. In plants and animals
with mosaic genomic methylation, functionally mysterious methylation is also common
within constitutively active housekeeping genes. Here, we show that H1 is enriched
in methylated sequences, including genes, of Arabidopsis thaliana, yet this enrichment
is independent of DNA methylation. Loss of H1 disperses heterochromatin, globally
alters nucleosome organization, and activates H1-bound genes, but only weakly
de-represses transposable elements. However, H1 loss strongly activates transposable
elements hypomethylated through mutation of DNA methyltransferase MET1. Hypomethylation
of genes also activates antisense transcription, which is modestly enhanced by
H1 loss. Our results demonstrate that H1 and DNA methylation jointly maintain
transcriptional homeostasis by silencing transposable elements and aberrant intragenic
transcripts. Such functionality plausibly explains why DNA methylation, a well-known
mutagen, has been maintained within coding sequences of crucial plant and animal
genes.
article_processing_charge: No
article_type: original
author:
- first_name: Jaemyung
full_name: Choi, Jaemyung
last_name: Choi
- first_name: David B.
full_name: Lyons, David B.
last_name: Lyons
- first_name: M. Yvonne
full_name: Kim, M. Yvonne
last_name: Kim
- first_name: Jonathan D.
full_name: Moore, Jonathan D.
last_name: Moore
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
citation:
ama: Choi J, Lyons DB, Kim MY, Moore JD, Zilberman D. DNA methylation and histone
H1 jointly repress transposable elements and aberrant intragenic transcripts.
Molecular Cell. 2020;77(2):310-323.e7. doi:10.1016/j.molcel.2019.10.011
apa: Choi, J., Lyons, D. B., Kim, M. Y., Moore, J. D., & Zilberman, D. (2020).
DNA methylation and histone H1 jointly repress transposable elements and aberrant
intragenic transcripts. Molecular Cell. Elsevier. https://doi.org/10.1016/j.molcel.2019.10.011
chicago: Choi, Jaemyung, David B. Lyons, M. Yvonne Kim, Jonathan D. Moore, and Daniel
Zilberman. “DNA Methylation and Histone H1 Jointly Repress Transposable Elements
and Aberrant Intragenic Transcripts.” Molecular Cell. Elsevier, 2020. https://doi.org/10.1016/j.molcel.2019.10.011.
ieee: J. Choi, D. B. Lyons, M. Y. Kim, J. D. Moore, and D. Zilberman, “DNA methylation
and histone H1 jointly repress transposable elements and aberrant intragenic transcripts,”
Molecular Cell, vol. 77, no. 2. Elsevier, p. 310–323.e7, 2020.
ista: Choi J, Lyons DB, Kim MY, Moore JD, Zilberman D. 2020. DNA methylation and
histone H1 jointly repress transposable elements and aberrant intragenic transcripts.
Molecular Cell. 77(2), 310–323.e7.
mla: Choi, Jaemyung, et al. “DNA Methylation and Histone H1 Jointly Repress Transposable
Elements and Aberrant Intragenic Transcripts.” Molecular Cell, vol. 77,
no. 2, Elsevier, 2020, p. 310–323.e7, doi:10.1016/j.molcel.2019.10.011.
short: J. Choi, D.B. Lyons, M.Y. Kim, J.D. Moore, D. Zilberman, Molecular Cell 77
(2020) 310–323.e7.
date_created: 2021-06-08T06:37:09Z
date_published: 2020-01-16T00:00:00Z
date_updated: 2024-10-16T12:14:37Z
day: '16'
department:
- _id: DaZi
doi: 10.1016/j.molcel.2019.10.011
extern: '1'
external_id:
pmid:
- '31732458'
intvolume: ' 77'
issue: '2'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.molcel.2019.10.011
month: '01'
oa: 1
oa_version: Published Version
page: 310-323.e7
pmid: 1
publication: Molecular Cell
publication_identifier:
eissn:
- 1097-4164
issn:
- 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: DNA methylation and histone H1 jointly repress transposable elements and aberrant
intragenic transcripts
type: journal_article
user_id: 0043cee0-e5fc-11ee-9736-f83bc23afbf0
volume: 77
year: '2020'
...
---
_id: '7395'
abstract:
- lang: eng
text: The mitochondrial electron transport chain complexes are organized into supercomplexes
(SCs) of defined stoichiometry, which have been proposed to regulate electron
flux via substrate channeling. We demonstrate that CoQ trapping in the isolated
SC I+III2 limits complex (C)I turnover, arguing against channeling. The SC structure,
resolved at up to 3.8 Å in four distinct states, suggests that CoQ oxidation may
be rate limiting because of unequal access of CoQ to the active sites of CIII2.
CI shows a transition between “closed” and “open” conformations, accompanied by
the striking rotation of a key transmembrane helix. Furthermore, the state of
CI affects the conformational flexibility within CIII2, demonstrating crosstalk
between the enzymes. CoQ was identified at only three of the four binding sites
in CIII2, suggesting that interaction with CI disrupts CIII2 symmetry in a functionally
relevant manner. Together, these observations indicate a more nuanced functional
role for the SCs.
article_processing_charge: No
article_type: original
author:
- first_name: James A
full_name: Letts, James A
id: 322DA418-F248-11E8-B48F-1D18A9856A87
last_name: Letts
orcid: 0000-0002-9864-3586
- first_name: Karol
full_name: Fiedorczuk, Karol
id: 5BFF67CE-02D1-11E9-B11A-A5A4D7DFFFD0
last_name: Fiedorczuk
- first_name: Gianluca
full_name: Degliesposti, Gianluca
last_name: Degliesposti
- first_name: Mark
full_name: Skehel, Mark
last_name: Skehel
- first_name: Leonid A
full_name: Sazanov, Leonid A
id: 338D39FE-F248-11E8-B48F-1D18A9856A87
last_name: Sazanov
orcid: 0000-0002-0977-7989
citation:
ama: Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA. Structures of
respiratory supercomplex I+III2 reveal functional and conformational crosstalk.
Molecular Cell. 2019;75(6):1131-1146.e6. doi:10.1016/j.molcel.2019.07.022
apa: Letts, J. A., Fiedorczuk, K., Degliesposti, G., Skehel, M., & Sazanov,
L. A. (2019). Structures of respiratory supercomplex I+III2 reveal functional
and conformational crosstalk. Molecular Cell. Cell Press. https://doi.org/10.1016/j.molcel.2019.07.022
chicago: Letts, James A, Karol Fiedorczuk, Gianluca Degliesposti, Mark Skehel, and
Leonid A Sazanov. “Structures of Respiratory Supercomplex I+III2 Reveal Functional
and Conformational Crosstalk.” Molecular Cell. Cell Press, 2019. https://doi.org/10.1016/j.molcel.2019.07.022.
ieee: J. A. Letts, K. Fiedorczuk, G. Degliesposti, M. Skehel, and L. A. Sazanov,
“Structures of respiratory supercomplex I+III2 reveal functional and conformational
crosstalk,” Molecular Cell, vol. 75, no. 6. Cell Press, p. 1131–1146.e6,
2019.
ista: Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA. 2019. Structures
of respiratory supercomplex I+III2 reveal functional and conformational crosstalk.
Molecular Cell. 75(6), 1131–1146.e6.
mla: Letts, James A., et al. “Structures of Respiratory Supercomplex I+III2 Reveal
Functional and Conformational Crosstalk.” Molecular Cell, vol. 75, no.
6, Cell Press, 2019, p. 1131–1146.e6, doi:10.1016/j.molcel.2019.07.022.
short: J.A. Letts, K. Fiedorczuk, G. Degliesposti, M. Skehel, L.A. Sazanov, Molecular
Cell 75 (2019) 1131–1146.e6.
corr_author: '1'
date_created: 2020-01-29T16:02:33Z
date_published: 2019-09-19T00:00:00Z
date_updated: 2024-10-22T09:34:12Z
day: '19'
ddc:
- '570'
department:
- _id: LeSa
doi: 10.1016/j.molcel.2019.07.022
ec_funded: 1
external_id:
isi:
- '000486614200006'
pmid:
- '31492636'
file:
- access_level: open_access
checksum: 5202f53a237d6650ece038fbf13bdcea
content_type: application/pdf
creator: dernst
date_created: 2020-02-04T10:37:28Z
date_updated: 2020-07-14T12:47:57Z
file_id: '7447'
file_name: 2019_MolecularCell_Letts.pdf
file_size: 9654895
relation: main_file
file_date_updated: 2020-07-14T12:47:57Z
has_accepted_license: '1'
intvolume: ' 75'
isi: 1
issue: '6'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
page: 1131-1146.e6
pmid: 1
project:
- _id: 2590DB08-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '701309'
name: Atomic Resolution Structures of Mitochondrial Respiratory Chain Supercomplexes
publication: Molecular Cell
publication_identifier:
issn:
- 1097-2765
publication_status: published
publisher: Cell Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structures of respiratory supercomplex I+III2 reveal functional and conformational
crosstalk
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: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 75
year: '2019'
...
---
_id: '15155'
abstract:
- lang: eng
text: The C-terminal transactivation domain (TAD) of BMAL1 (brain and muscle ARNT-like
1) is a regulatory hub for transcriptional coactivators and repressors that compete
for binding and, consequently, contributes to period determination of the mammalian
circadian clock. Here, we report the discovery of two distinct conformational
states that slowly exchange within the dynamic TAD to control timing. This binary
switch results from cis/trans isomerization about a highly conserved Trp-Pro imide
bond in a region of the TAD that is required for normal circadian timekeeping.
Both cis and trans isomers interact with transcriptional regulators, suggesting
that isomerization could serve a role in assembling regulatory complexes in vivo.
Toward this end, we show that locking the switch into the trans isomer leads to
shortened circadian periods. Furthermore, isomerization is regulated by the cyclophilin
family of peptidyl-prolyl isomerases, highlighting the potential for regulation
of BMAL1 protein dynamics in period determination.
article_processing_charge: No
article_type: original
author:
- first_name: Chelsea L.
full_name: Gustafson, Chelsea L.
last_name: Gustafson
- first_name: Nicole C.
full_name: Parsley, Nicole C.
last_name: Parsley
- first_name: Hande
full_name: Asimgil, Hande
last_name: Asimgil
- first_name: Hsiau-Wei
full_name: Lee, Hsiau-Wei
last_name: Lee
- first_name: Christopher
full_name: Ahlbach, Christopher
last_name: Ahlbach
- first_name: Alicia Kathleen
full_name: Michael, Alicia Kathleen
id: 6437c950-2a03-11ee-914d-d6476dd7b75c
last_name: Michael
- first_name: Haiyan
full_name: Xu, Haiyan
last_name: Xu
- first_name: Owen L.
full_name: Williams, Owen L.
last_name: Williams
- first_name: Tara L.
full_name: Davis, Tara L.
last_name: Davis
- first_name: Andrew C.
full_name: Liu, Andrew C.
last_name: Liu
- first_name: Carrie L.
full_name: Partch, Carrie L.
last_name: Partch
citation:
ama: Gustafson CL, Parsley NC, Asimgil H, et al. A slow conformational switch in
the BMAL1 transactivation domain modulates circadian rhythms. Molecular Cell.
2017;66(4):447-457.e7. doi:10.1016/j.molcel.2017.04.011
apa: Gustafson, C. L., Parsley, N. C., Asimgil, H., Lee, H.-W., Ahlbach, C., Michael,
A. K., … Partch, C. L. (2017). A slow conformational switch in the BMAL1 transactivation
domain modulates circadian rhythms. Molecular Cell. Elsevier. https://doi.org/10.1016/j.molcel.2017.04.011
chicago: Gustafson, Chelsea L., Nicole C. Parsley, Hande Asimgil, Hsiau-Wei Lee,
Christopher Ahlbach, Alicia K. Michael, Haiyan Xu, et al. “A Slow Conformational
Switch in the BMAL1 Transactivation Domain Modulates Circadian Rhythms.” Molecular
Cell. Elsevier, 2017. https://doi.org/10.1016/j.molcel.2017.04.011.
ieee: C. L. Gustafson et al., “A slow conformational switch in the BMAL1
transactivation domain modulates circadian rhythms,” Molecular Cell, vol.
66, no. 4. Elsevier, p. 447–457.e7, 2017.
ista: Gustafson CL, Parsley NC, Asimgil H, Lee H-W, Ahlbach C, Michael AK, Xu H,
Williams OL, Davis TL, Liu AC, Partch CL. 2017. A slow conformational switch in
the BMAL1 transactivation domain modulates circadian rhythms. Molecular Cell.
66(4), 447–457.e7.
mla: Gustafson, Chelsea L., et al. “A Slow Conformational Switch in the BMAL1 Transactivation
Domain Modulates Circadian Rhythms.” Molecular Cell, vol. 66, no. 4, Elsevier,
2017, p. 447–457.e7, doi:10.1016/j.molcel.2017.04.011.
short: C.L. Gustafson, N.C. Parsley, H. Asimgil, H.-W. Lee, C. Ahlbach, A.K. Michael,
H. Xu, O.L. Williams, T.L. Davis, A.C. Liu, C.L. Partch, Molecular Cell 66 (2017)
447–457.e7.
date_created: 2024-03-21T07:56:01Z
date_published: 2017-05-18T00:00:00Z
date_updated: 2024-03-25T12:19:20Z
day: '18'
doi: 10.1016/j.molcel.2017.04.011
extern: '1'
intvolume: ' 66'
issue: '4'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.molcel.2017.04.011
month: '05'
oa: 1
oa_version: Published Version
page: 447-457.e7
publication: Molecular Cell
publication_identifier:
issn:
- 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: A slow conformational switch in the BMAL1 transactivation domain modulates
circadian rhythms
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 66
year: '2017'
...
---
_id: '15160'
abstract:
- lang: eng
text: The circadian clock orchestrates global changes in transcriptional regulation
on a daily basis via the bHLH-PAS transcription factor CLOCK:BMAL1. Pathways driven
by other bHLH-PAS transcription factors have a homologous repressor that modulates
activity on a tissue-specific basis, but none have been identified for CLOCK:BMAL1.
We show here that the cancer/testis antigen PASD1 fulfills this role to suppress
circadian rhythms. PASD1 is evolutionarily related to CLOCK and interacts with
the CLOCK:BMAL1 complex to repress transcriptional activation. Expression of PASD1
is restricted to germline tissues in healthy individuals but can be induced in
cells of somatic origin upon oncogenic transformation. Reducing PASD1 in human
cancer cells significantly increases the amplitude of transcriptional oscillations
to generate more robust circadian rhythms. Our results describe a function for
a germline-specific protein in regulation of the circadian clock and provide a
molecular link from oncogenic transformation to suppression of circadian rhythms.
article_processing_charge: No
article_type: original
author:
- first_name: Alicia Kathleen
full_name: Michael, Alicia Kathleen
id: 6437c950-2a03-11ee-914d-d6476dd7b75c
last_name: Michael
- first_name: Stacy L.
full_name: Harvey, Stacy L.
last_name: Harvey
- first_name: Patrick J.
full_name: Sammons, Patrick J.
last_name: Sammons
- first_name: Amanda P.
full_name: Anderson, Amanda P.
last_name: Anderson
- first_name: Hema M.
full_name: Kopalle, Hema M.
last_name: Kopalle
- first_name: Alison H.
full_name: Banham, Alison H.
last_name: Banham
- first_name: Carrie L.
full_name: Partch, Carrie L.
last_name: Partch
citation:
ama: Michael AK, Harvey SL, Sammons PJ, et al. Cancer/Testis antigen PASD1 silences
the circadian clock. Molecular Cell. 2015;58(5):743-754. doi:10.1016/j.molcel.2015.03.031
apa: Michael, A. K., Harvey, S. L., Sammons, P. J., Anderson, A. P., Kopalle, H.
M., Banham, A. H., & Partch, C. L. (2015). Cancer/Testis antigen PASD1 silences
the circadian clock. Molecular Cell. Elsevier. https://doi.org/10.1016/j.molcel.2015.03.031
chicago: Michael, Alicia K., Stacy L. Harvey, Patrick J. Sammons, Amanda P. Anderson,
Hema M. Kopalle, Alison H. Banham, and Carrie L. Partch. “Cancer/Testis Antigen
PASD1 Silences the Circadian Clock.” Molecular Cell. Elsevier, 2015. https://doi.org/10.1016/j.molcel.2015.03.031.
ieee: A. K. Michael et al., “Cancer/Testis antigen PASD1 silences the circadian
clock,” Molecular Cell, vol. 58, no. 5. Elsevier, pp. 743–754, 2015.
ista: Michael AK, Harvey SL, Sammons PJ, Anderson AP, Kopalle HM, Banham AH, Partch
CL. 2015. Cancer/Testis antigen PASD1 silences the circadian clock. Molecular
Cell. 58(5), 743–754.
mla: Michael, Alicia K., et al. “Cancer/Testis Antigen PASD1 Silences the Circadian
Clock.” Molecular Cell, vol. 58, no. 5, Elsevier, 2015, pp. 743–54, doi:10.1016/j.molcel.2015.03.031.
short: A.K. Michael, S.L. Harvey, P.J. Sammons, A.P. Anderson, H.M. Kopalle, A.H.
Banham, C.L. Partch, Molecular Cell 58 (2015) 743–754.
date_created: 2024-03-21T07:58:08Z
date_published: 2015-06-04T00:00:00Z
date_updated: 2024-03-25T11:52:26Z
day: '04'
doi: 10.1016/j.molcel.2015.03.031
extern: '1'
intvolume: ' 58'
issue: '5'
keyword:
- Cell Biology
- Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.molcel.2015.03.031
month: '06'
oa: 1
oa_version: Published Version
page: 743-754
publication: Molecular Cell
publication_identifier:
issn:
- 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Cancer/Testis antigen PASD1 silences the circadian clock
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 58
year: '2015'
...
---
_id: '11127'
abstract:
- lang: eng
text: Nuclear formation in Xenopus egg extracts requires cytosol and is inhibited
by GTPγS, indicating a requirement for GTPase activity. Nuclear envelope (NE)
vesicle fusion is extensively inhibited by GTPγS and two mutant forms of the Ran
GTPase, Q69L and T24N. Depletion of either Ran or RCC1, the exchange factor for
Ran, from the assembly reaction also inhibits this step of NE formation. Ran depletion
can be complemented by the addition of Ran loaded with either GTP or GDP but not
with GTPγS. RCC1 depletion is only complemented by RCC1 itself or by RanGTP. Thus,
generation of RanGTP by RCC1 and GTP hydrolysis by Ran are both required for the
extensive membrane fusion events that lead to NE formation.
article_processing_charge: No
article_type: original
author:
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
- first_name: Daniel
full_name: Bilbao-Cortés, Daniel
last_name: Bilbao-Cortés
- first_name: Tobias C
full_name: Walther, Tobias C
last_name: Walther
- first_name: Oliver J
full_name: Gruss, Oliver J
last_name: Gruss
- first_name: Iain W
full_name: Mattaj, Iain W
last_name: Mattaj
citation:
ama: Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. GTP hydrolysis
by Ran is required for nuclear envelope assembly. Molecular Cell. 2000;5(6):1013-1024.
doi:10.1016/s1097-2765(00)80266-x
apa: Hetzer, M., Bilbao-Cortés, D., Walther, T. C., Gruss, O. J., & Mattaj,
I. W. (2000). GTP hydrolysis by Ran is required for nuclear envelope assembly.
Molecular Cell. Elsevier. https://doi.org/10.1016/s1097-2765(00)80266-x
chicago: Hetzer, Martin, Daniel Bilbao-Cortés, Tobias C Walther, Oliver J Gruss,
and Iain W Mattaj. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope Assembly.”
Molecular Cell. Elsevier, 2000. https://doi.org/10.1016/s1097-2765(00)80266-x.
ieee: M. Hetzer, D. Bilbao-Cortés, T. C. Walther, O. J. Gruss, and I. W. Mattaj,
“GTP hydrolysis by Ran is required for nuclear envelope assembly,” Molecular
Cell, vol. 5, no. 6. Elsevier, pp. 1013–1024, 2000.
ista: Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. 2000. GTP hydrolysis
by Ran is required for nuclear envelope assembly. Molecular Cell. 5(6), 1013–1024.
mla: Hetzer, Martin, et al. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope
Assembly.” Molecular Cell, vol. 5, no. 6, Elsevier, 2000, pp. 1013–24,
doi:10.1016/s1097-2765(00)80266-x.
short: M. Hetzer, D. Bilbao-Cortés, T.C. Walther, O.J. Gruss, I.W. Mattaj, Molecular
Cell 5 (2000) 1013–1024.
date_created: 2022-04-07T07:57:59Z
date_published: 2000-06-01T00:00:00Z
date_updated: 2022-07-18T08:58:31Z
day: '01'
doi: 10.1016/s1097-2765(00)80266-x
extern: '1'
external_id:
pmid:
- '10911995'
intvolume: ' 5'
issue: '6'
keyword:
- Cell Biology
- Molecular Biology
language:
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main_file_link:
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url: https://doi.org/10.1016/S1097-2765(00)80266-X
month: '06'
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oa_version: Published Version
page: 1013-1024
pmid: 1
publication: Molecular Cell
publication_identifier:
issn:
- 1097-2765
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: GTP hydrolysis by Ran is required for nuclear envelope assembly
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 5
year: '2000'
...