---
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. <i>Nature Structural &#38; Molecular
    Biology</i>. 2025;32:607-612. doi:<a href="https://doi.org/10.1038/s41594-024-01448-7">10.1038/s41594-024-01448-7</a>
  apa: Tluckova, K., Kaczmarek, B. M., Testa Salmazo, A. P., &#38; Bernecky, C. (2025).
    Mechanism of mammalian transcriptional repression by noncoding RNA. <i>Nature
    Structural &#38; Molecular Biology</i>. Springer Nature. <a href="https://doi.org/10.1038/s41594-024-01448-7">https://doi.org/10.1038/s41594-024-01448-7</a>
  chicago: Tluckova, Katarina, Beata M Kaczmarek, Anita P Testa Salmazo, and Carrie
    Bernecky. “Mechanism of Mammalian Transcriptional Repression by Noncoding RNA.”
    <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2025. <a href="https://doi.org/10.1038/s41594-024-01448-7">https://doi.org/10.1038/s41594-024-01448-7</a>.
  ieee: K. Tluckova, B. M. Kaczmarek, A. P. Testa Salmazo, and C. Bernecky, “Mechanism
    of mammalian transcriptional repression by noncoding RNA,” <i>Nature Structural
    &#38; Molecular Biology</i>, 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 &#38;
    Molecular Biology. 32, 607–612.
  mla: Tluckova, Katarina, et al. “Mechanism of Mammalian Transcriptional Repression
    by Noncoding RNA.” <i>Nature Structural &#38; Molecular Biology</i>, vol. 32,
    Springer Nature, 2025, pp. 607–12, doi:<a href="https://doi.org/10.1038/s41594-024-01448-7">10.1038/s41594-024-01448-7</a>.
  short: K. Tluckova, B.M. Kaczmarek, A.P. Testa Salmazo, C. Bernecky, Nature Structural
    &#38; 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:
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  date_updated: 2025-04-16T08:17:27Z
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  file_size: 9306639
  relation: main_file
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file_date_updated: 2025-04-16T08:17:27Z
fulldoi: https://doi.org/10.1038/s41594-024-01448-7
has_accepted_license: '1'
intvolume: '        32'
isi: 1
language:
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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:
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    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'
...
---
APC_amount: 12348 EUR
OA_place: publisher
OA_type: hybrid
_id: '17884'
abstract:
- lang: eng
  text: Human T cell leukemia virus type 1 (HTLV-1) immature particles differ in morphology
    from other retroviruses, suggesting a distinct way of assembly. Here we report
    the results of cryo-electron tomography studies of HTLV-1 virus-like particles
    assembled in vitro, as well as derived from cells. This work shows that HTLV-1
    uses a distinct mechanism of Gag–Gag interactions to form the immature viral lattice.
    Analysis of high-resolution structural information from immature capsid (CA) tubular
    arrays reveals that the primary stabilizing component in HTLV-1 is the N-terminal
    domain of CA. Mutagenesis analysis supports this observation. This distinguishes
    HTLV-1 from other retroviruses, in which the stabilization is provided primarily
    by the C-terminal domain of CA. These results provide structural details of the
    quaternary arrangement of Gag for an immature deltaretrovirus and this helps explain
    why HTLV-1 particles are morphologically distinct.
acknowledged_ssus:
- _id: ScienComp
- _id: LifeSc
- _id: EM-Fac
acknowledgement: This work was funded by the Institute of Science and Technology Austria
  (ISTA) and the Austrian Science Fund (grant P31445 to F.K.M.S.). Access to high-resolution
  cryo-ET data acquisition at European Molecular Biology Laboratory (EMBL) Heidelberg
  was supported through the EMBL cryo-EM platform. We thank V.-V. Hodirnau at ISTA
  and W. Hagen and F. Weis at EMBL Heidelberg for support in cryo-ET data acquisition.
  This research was also supported by the scientific service units of ISTA through
  resources provided by Scientific Computing, the Life Science Facility, and the EM
  Facility. L.M.M. was supported by National Institutes of Health grants R01 GM151775
  and R21 DE032878 and by the University of Minnesota Masonic Cancer Center. D.P.
  was supported by the DOC doctoral fellowship program of the Austrian Academy of
  Sciences. R.A.D was supported by the National Institute of Allergy and Infectious
  Diseases (grant R01AI147890). The funders had no role in study design, data collection
  and analysis, decision to publish or preparation of the manuscript. Specifically,
  we also want to thank A. Schlögl for computational support and J. Hansen and V.
  Vogt for critical comments on the manuscript. We also thank the other members of
  the Schur lab for helpful discussions and experimental advice.
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Martin
  full_name: Obr, Martin
  id: 4741CA5A-F248-11E8-B48F-1D18A9856A87
  last_name: Obr
  orcid: 0000-0003-1756-6564
- first_name: Mathias
  full_name: Percipalle, Mathias
  id: 4986e21c-eb97-11eb-a6c2-a4ef0b629971
  last_name: Percipalle
- first_name: Darya
  full_name: Chernikova, Darya
  id: 7dbaf460-fa9e-11eb-b0ca-bc7c7ff21ad0
  last_name: Chernikova
- first_name: Huixin
  full_name: Yang, Huixin
  last_name: Yang
- first_name: Andreas
  full_name: Thader, Andreas
  id: 3A18A7B8-F248-11E8-B48F-1D18A9856A87
  last_name: Thader
- first_name: Gergely
  full_name: Pinke, Gergely
  id: 4D5303E6-F248-11E8-B48F-1D18A9856A87
  last_name: Pinke
- first_name: Dario J
  full_name: Porley, Dario J
  id: 2FD6EA6C-F248-11E8-B48F-1D18A9856A87
  last_name: Porley
- first_name: Louis M.
  full_name: Mansky, Louis M.
  last_name: Mansky
- first_name: Robert A.
  full_name: Dick, Robert A.
  last_name: Dick
- first_name: Florian KM
  full_name: Schur, Florian KM
  id: 48AD8942-F248-11E8-B48F-1D18A9856A87
  last_name: Schur
  orcid: 0000-0003-4790-8078
citation:
  ama: Obr M, Percipalle M, Chernikova D, et al. Distinct stabilization of the human
    T cell leukemia virus type 1 immature Gag lattice. <i>Nature Structural &#38;
    Molecular Biology</i>. 2025;32:268-276. doi:<a href="https://doi.org/10.1038/s41594-024-01390-8">10.1038/s41594-024-01390-8</a>
  apa: Obr, M., Percipalle, M., Chernikova, D., Yang, H., Thader, A., Pinke, G., …
    Schur, F. K. (2025). Distinct stabilization of the human T cell leukemia virus
    type 1 immature Gag lattice. <i>Nature Structural &#38; Molecular Biology</i>.
    Springer Nature. <a href="https://doi.org/10.1038/s41594-024-01390-8">https://doi.org/10.1038/s41594-024-01390-8</a>
  chicago: Obr, Martin, Mathias Percipalle, Darya Chernikova, Huixin Yang, Andreas
    Thader, Gergely Pinke, Darío Porley Esteves, Louis M. Mansky, Robert A. Dick,
    and Florian KM Schur. “Distinct Stabilization of the Human T Cell Leukemia Virus
    Type 1 Immature Gag Lattice.” <i>Nature Structural &#38; Molecular Biology</i>.
    Springer Nature, 2025. <a href="https://doi.org/10.1038/s41594-024-01390-8">https://doi.org/10.1038/s41594-024-01390-8</a>.
  ieee: M. Obr <i>et al.</i>, “Distinct stabilization of the human T cell leukemia
    virus type 1 immature Gag lattice,” <i>Nature Structural &#38; Molecular Biology</i>,
    vol. 32. Springer Nature, pp. 268–276, 2025.
  ista: Obr M, Percipalle M, Chernikova D, Yang H, Thader A, Pinke G, Porley Esteves
    D, Mansky LM, Dick RA, Schur FK. 2025. Distinct stabilization of the human T cell
    leukemia virus type 1 immature Gag lattice. Nature Structural &#38; Molecular
    Biology. 32, 268–276.
  mla: Obr, Martin, et al. “Distinct Stabilization of the Human T Cell Leukemia Virus
    Type 1 Immature Gag Lattice.” <i>Nature Structural &#38; Molecular Biology</i>,
    vol. 32, Springer Nature, 2025, pp. 268–76, doi:<a href="https://doi.org/10.1038/s41594-024-01390-8">10.1038/s41594-024-01390-8</a>.
  short: M. Obr, M. Percipalle, D. Chernikova, H. Yang, A. Thader, G. Pinke, D. Porley
    Esteves, L.M. Mansky, R.A. Dick, F.K. Schur, Nature Structural &#38; Molecular
    Biology 32 (2025) 268–276.
corr_author: '1'
date_created: 2024-09-08T10:29:06Z
date_published: 2025-02-01T00:00:00Z
date_updated: 2026-03-16T12:55:18Z
day: '01'
ddc:
- '570'
department:
- _id: FlSc
- _id: LeSa
doi: 10.1038/s41594-024-01390-8
external_id:
  isi:
  - '001306564000001'
  oaworkid:
  - W4402316284
  pmid:
  - '39242978'
file:
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  checksum: c641ad94afb28917b20425db676fc3ee
  content_type: application/pdf
  creator: dernst
  date_created: 2025-04-23T07:02:33Z
  date_updated: 2025-04-23T07:02:33Z
  file_id: '19608'
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  relation: main_file
  success: 1
file_date_updated: 2025-04-23T07:02:33Z
fulldoi: https://doi.org/10.1038/s41594-024-01390-8
has_accepted_license: '1'
intvolume: '        32'
isi: 1
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
oaworkid: 1
page: 268-276
pmid: 1
project:
- _id: 26736D6A-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: P31445
  name: Structural conservation and diversity in retroviral capsid
- _id: 9B9C98E0-BA93-11EA-9121-9846C619BF3A
  grant_number: '25762'
  name: Structural characterization of spumavirus capsid assemblies to understand
    conserved Ortervirales assembly mechanisms
publication: Nature Structural & Molecular Biology
publication_identifier:
  eissn:
  - 1545-9985
  issn:
  - 1545-9993
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Distinct stabilization of the human T cell leukemia virus type 1 immature Gag
  lattice
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'
...
---
APC_amount: 11700 EUR
OA_place: publisher
OA_type: hybrid
_id: '14979'
abstract:
- lang: eng
  text: Poxviruses are among the largest double-stranded DNA viruses, with members
    such as variola virus, monkeypox virus and the vaccination strain vaccinia virus
    (VACV). Knowledge about the structural proteins that form the viral core has remained
    sparse. While major core proteins have been annotated via indirect experimental
    evidence, their structures have remained elusive and they could not be assigned
    to individual core features. Hence, which proteins constitute which layers of
    the core, such as the palisade layer and the inner core wall, has remained enigmatic.
    Here we show, using a multi-modal cryo-electron microscopy (cryo-EM) approach
    in combination with AlphaFold molecular modeling, that trimers formed by the cleavage
    product of VACV protein A10 are the key component of the palisade layer. This
    allows us to place previously obtained descriptions of protein interactions within
    the core wall into perspective and to provide a detailed model of poxvirus core
    architecture. Importantly, we show that interactions within A10 trimers are likely
    generalizable over members of orthopox- and parapoxviruses.
acknowledged_ssus:
- _id: ScienComp
- _id: LifeSc
- _id: EM-Fac
acknowledgement: "We thank A. Bergthaler (Research Center for Molecular Medicine of
  the Austrian Academy of Sciences) for providing VACV WR. We thank A. Nicholas and
  his team at the ISTA proteomics facility, and S. Elefante at the ISTA Scientific
  Computing facility for their support. We also thank F. Fäßler, D. Porley, T. Muthspiel
  and other members of the Schur group for support and helpful discussions. We also
  thank D. Castaño-Díez for support with Dynamo. We thank D. Farrell for his help
  optimizing the Rosetta protocol to refine the atomic model into the cryo-EM map
  with symmetry.\r\n\r\nF.K.M.S. acknowledges support from ISTA and EMBO. F.K.M.S.
  also received support from the Austrian Science Fund (FWF) grant P31445. This publication
  has been made possible in part by CZI grant DAF2021-234754 and grant https://doi.org/10.37921/812628ebpcwg
  from the Chan Zuckerberg Initiative DAF, an advised fund of Silicon Valley Community
  Foundation (funder https://doi.org/10.13039/100014989) awarded to F.K.M.S.\r\n\r\nThis
  research was also supported by the Scientific Service Units (SSUs) of ISTA through
  resources provided by Scientific Computing (SciComp), the Life Science Facility
  (LSF), and the Electron Microscopy Facility (EMF). We also acknowledge the use of
  COSMIC45 and Colabfold46."
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Julia
  full_name: Datler, Julia
  id: 3B12E2E6-F248-11E8-B48F-1D18A9856A87
  last_name: Datler
  orcid: 0000-0002-3616-8580
- first_name: Jesse
  full_name: Hansen, Jesse
  id: 1063c618-6f9b-11ec-9123-f912fccded63
  last_name: Hansen
  orcid: 0000-0001-7967-2085
- first_name: Andreas
  full_name: Thader, Andreas
  id: 3A18A7B8-F248-11E8-B48F-1D18A9856A87
  last_name: Thader
- first_name: Alois
  full_name: Schlögl, Alois
  id: 45BF87EE-F248-11E8-B48F-1D18A9856A87
  last_name: Schlögl
  orcid: 0000-0002-5621-8100
- first_name: Lukas W
  full_name: Bauer, Lukas W
  id: 0c894dcf-897b-11ed-a09c-8186353224b0
  last_name: Bauer
- first_name: Victor-Valentin
  full_name: Hodirnau, Victor-Valentin
  id: 3661B498-F248-11E8-B48F-1D18A9856A87
  last_name: Hodirnau
  orcid: 0000-0003-3904-947X
- first_name: Florian KM
  full_name: Schur, Florian KM
  id: 48AD8942-F248-11E8-B48F-1D18A9856A87
  last_name: Schur
  orcid: 0000-0003-4790-8078
citation:
  ama: Datler J, Hansen J, Thader A, et al. Multi-modal cryo-EM reveals trimers of
    protein A10 to form the palisade layer in poxvirus cores. <i>Nature Structural
    &#38; Molecular Biology</i>. 2024;31:1114-1123. doi:<a href="https://doi.org/10.1038/s41594-023-01201-6">10.1038/s41594-023-01201-6</a>
  apa: Datler, J., Hansen, J., Thader, A., Schlögl, A., Bauer, L. W., Hodirnau, V.-V.,
    &#38; Schur, F. K. (2024). Multi-modal cryo-EM reveals trimers of protein A10
    to form the palisade layer in poxvirus cores. <i>Nature Structural &#38; Molecular
    Biology</i>. Springer Nature. <a href="https://doi.org/10.1038/s41594-023-01201-6">https://doi.org/10.1038/s41594-023-01201-6</a>
  chicago: Datler, Julia, Jesse Hansen, Andreas Thader, Alois Schlögl, Lukas W Bauer,
    Victor-Valentin Hodirnau, and Florian KM Schur. “Multi-Modal Cryo-EM Reveals Trimers
    of Protein A10 to Form the Palisade Layer in Poxvirus Cores.” <i>Nature Structural
    &#38; Molecular Biology</i>. Springer Nature, 2024. <a href="https://doi.org/10.1038/s41594-023-01201-6">https://doi.org/10.1038/s41594-023-01201-6</a>.
  ieee: J. Datler <i>et al.</i>, “Multi-modal cryo-EM reveals trimers of protein A10
    to form the palisade layer in poxvirus cores,” <i>Nature Structural &#38; Molecular
    Biology</i>, vol. 31. Springer Nature, pp. 1114–1123, 2024.
  ista: Datler J, Hansen J, Thader A, Schlögl A, Bauer LW, Hodirnau V-V, Schur FK.
    2024. Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade
    layer in poxvirus cores. Nature Structural &#38; Molecular Biology. 31, 1114–1123.
  mla: Datler, Julia, et al. “Multi-Modal Cryo-EM Reveals Trimers of Protein A10 to
    Form the Palisade Layer in Poxvirus Cores.” <i>Nature Structural &#38; Molecular
    Biology</i>, vol. 31, Springer Nature, 2024, pp. 1114–23, doi:<a href="https://doi.org/10.1038/s41594-023-01201-6">10.1038/s41594-023-01201-6</a>.
  short: J. Datler, J. Hansen, A. Thader, A. Schlögl, L.W. Bauer, V.-V. Hodirnau,
    F.K. Schur, Nature Structural &#38; Molecular Biology 31 (2024) 1114–1123.
corr_author: '1'
date_created: 2024-02-12T09:59:45Z
date_published: 2024-07-01T00:00:00Z
date_updated: 2026-04-07T12:59:44Z
day: '01'
ddc:
- '570'
department:
- _id: FlSc
- _id: ScienComp
- _id: EM-Fac
doi: 10.1038/s41594-023-01201-6
external_id:
  isi:
  - '001158144600002'
  pmid:
  - '38316877'
file:
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  date_created: 2024-07-22T11:27:22Z
  date_updated: 2024-07-22T11:27:22Z
  file_id: '17307'
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  success: 1
file_date_updated: 2024-07-22T11:27:22Z
fulldoi: https://doi.org/10.1038/s41594-023-01201-6
has_accepted_license: '1'
intvolume: '        31'
isi: 1
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
page: 1114-1123
pmid: 1
project:
- _id: 26736D6A-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: P31445
  name: Structural conservation and diversity in retroviral capsid
publication: Nature Structural & Molecular Biology
publication_identifier:
  eissn:
  - 1545-9985
  issn:
  - 1545-9993
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
  link:
  - description: News on ISTA Website
    relation: press_release
    url: https://ista.ac.at/en/news/down-to-the-core-of-poxviruses/
  record:
  - id: '18766'
    relation: dissertation_contains
    status: public
scopus_import: '1'
status: public
title: Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade layer
  in poxvirus cores
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: 31
year: '2024'
...
---
OA_place: publisher
OA_type: hybrid
_id: '18645'
abstract:
- lang: eng
  text: Gene expression during natural and induced reprogramming is controlled by
    pioneer transcription factors that initiate transcription from closed chromatin.
    Nr5a2 is a key pioneer factor that regulates zygotic genome activation in totipotent
    embryos, pluripotency in embryonic stem cells and metabolism in adult tissues,
    but the mechanism of its pioneer activity remains poorly understood. Here, we
    present a cryo-electron microscopy structure of human NR5A2 bound to a nucleosome.
    The structure shows that the conserved carboxy-terminal extension (CTE) loop of
    the NR5A2 DNA-binding domain competes with a DNA minor groove anchor of the nucleosome
    and releases entry-exit site DNA. Mutational analysis showed that NR5A2 D159 of
    the CTE is dispensable for DNA binding but required for stable nucleosome association
    and persistent DNA ‘unwrapping’. These findings suggest that NR5A2 belongs to
    an emerging class of pioneer factors that can use DNA minor groove anchor competition
    to destabilize nucleosomes and facilitate gene expression during reprogramming.
acknowledgement: 'We are very grateful to K. Abe, L. G. Hernandez, C. Kobayashi, K.
  Straßer and M. Zaczek for their contributions and technical support. We thank N.
  Thomä for advice on SeEN-seq. We are grateful to A. Musacchio for insightful discussions.
  We thank J.-M. Peters for critical reading of the manuscript and all members of
  K.T.’s laboratory for discussions. We thank T. Schäfer at the cryo-EM facility for
  assistance in cryo-EM data collection, and R. H. Kim for sequencing at the NGS facility,
  MPIB. K.T. is an Honorary Professor at the Department of Biology, Ludwig-Maximilians-University,
  Munich. Funding: European Research Council grant ERC-CoG-818556 TotipotentZygotChrom
  (K.T.). European Research Council grant ERC-StG-804098 ReplisomeBypass (K.D.). Max
  Planck Society (K.T., K.D.).'
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Wataru
  full_name: Kobayashi, Wataru
  last_name: Kobayashi
- first_name: Anna H.
  full_name: Sappler, Anna H.
  last_name: Sappler
- first_name: Daniel
  full_name: Bollschweiler, Daniel
  last_name: Bollschweiler
- first_name: Maximilian
  full_name: Kümmecke, Maximilian
  last_name: Kümmecke
- first_name: Jérôme
  full_name: Basquin, Jérôme
  last_name: Basquin
- first_name: Eda Nur
  full_name: Arslantas, Eda Nur
  id: 36978b4e-2966-11ef-a72f-b3740ef1cd11
  last_name: Arslantas
- first_name: Siwat
  full_name: Ruangroengkulrith, Siwat
  last_name: Ruangroengkulrith
- first_name: Renate
  full_name: Hornberger, Renate
  last_name: Hornberger
- first_name: Karl
  full_name: Duderstadt, Karl
  last_name: Duderstadt
- first_name: Kikuë
  full_name: Tachibana, Kikuë
  last_name: Tachibana
citation:
  ama: Kobayashi W, Sappler AH, Bollschweiler D, et al. Nucleosome-bound NR5A2 structure
    reveals pioneer factor mechanism by DNA minor groove anchor competition. <i>Nature
    Structural &#38; Molecular Biology</i>. 2024;31:757-766. doi:<a href="https://doi.org/10.1038/s41594-024-01239-0">10.1038/s41594-024-01239-0</a>
  apa: Kobayashi, W., Sappler, A. H., Bollschweiler, D., Kümmecke, M., Basquin, J.,
    Arslantas, E. N., … Tachibana, K. (2024). Nucleosome-bound NR5A2 structure reveals
    pioneer factor mechanism by DNA minor groove anchor competition. <i>Nature Structural
    &#38; Molecular Biology</i>. Springer Nature. <a href="https://doi.org/10.1038/s41594-024-01239-0">https://doi.org/10.1038/s41594-024-01239-0</a>
  chicago: Kobayashi, Wataru, Anna H. Sappler, Daniel Bollschweiler, Maximilian Kümmecke,
    Jérôme Basquin, Eda Nur Arslantas, Siwat Ruangroengkulrith, Renate Hornberger,
    Karl Duderstadt, and Kikuë Tachibana. “Nucleosome-Bound NR5A2 Structure Reveals
    Pioneer Factor Mechanism by DNA Minor Groove Anchor Competition.” <i>Nature Structural
    &#38; Molecular Biology</i>. Springer Nature, 2024. <a href="https://doi.org/10.1038/s41594-024-01239-0">https://doi.org/10.1038/s41594-024-01239-0</a>.
  ieee: W. Kobayashi <i>et al.</i>, “Nucleosome-bound NR5A2 structure reveals pioneer
    factor mechanism by DNA minor groove anchor competition,” <i>Nature Structural
    &#38; Molecular Biology</i>, vol. 31. Springer Nature, pp. 757–766, 2024.
  ista: Kobayashi W, Sappler AH, Bollschweiler D, Kümmecke M, Basquin J, Arslantas
    EN, Ruangroengkulrith S, Hornberger R, Duderstadt K, Tachibana K. 2024. Nucleosome-bound
    NR5A2 structure reveals pioneer factor mechanism by DNA minor groove anchor competition.
    Nature Structural &#38; Molecular Biology. 31, 757–766.
  mla: Kobayashi, Wataru, et al. “Nucleosome-Bound NR5A2 Structure Reveals Pioneer
    Factor Mechanism by DNA Minor Groove Anchor Competition.” <i>Nature Structural
    &#38; Molecular Biology</i>, vol. 31, Springer Nature, 2024, pp. 757–66, doi:<a
    href="https://doi.org/10.1038/s41594-024-01239-0">10.1038/s41594-024-01239-0</a>.
  short: W. Kobayashi, A.H. Sappler, D. Bollschweiler, M. Kümmecke, J. Basquin, E.N.
    Arslantas, S. Ruangroengkulrith, R. Hornberger, K. Duderstadt, K. Tachibana, Nature
    Structural &#38; Molecular Biology 31 (2024) 757–766.
date_created: 2024-12-11T09:10:54Z
date_published: 2024-05-01T00:00:00Z
date_updated: 2024-12-11T10:56:35Z
day: '01'
doi: 10.1038/s41594-024-01239-0
extern: '1'
fulldoi: https://doi.org/10.1038/s41594-024-01239-0
intvolume: '        31'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1038/s41594-024-01239-0
month: '05'
oa: 1
oa_version: Published Version
page: 757-766
publication: Nature Structural & Molecular Biology
publication_identifier:
  eissn:
  - 1545-9985
  issn:
  - 1545-9993
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nucleosome-bound NR5A2 structure reveals pioneer factor mechanism by DNA minor
  groove anchor competition
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 31
year: '2024'
...
---
_id: '15323'
abstract:
- lang: eng
  text: Supercomplexes of the respiratory chain are established constituents of the
    oxidative phosphorylation system, but their role in mammalian metabolism has been
    hotly debated. Although recent studies have shown that different tissues/organs
    are equipped with specific sets of supercomplexes, depending on their metabolic
    needs, the notion that supercomplexes have a role in the regulation of metabolism
    has been challenged. However, irrespective of the mechanistic conclusions, the
    composition of various high molecular weight supercomplexes remains uncertain.
    Here, using cryogenic electron microscopy, we demonstrate that mammalian (mouse)
    tissues contain three defined types of ‘respirasome’, supercomplexes made of CI,
    CIII2 and CIV. The stoichiometry and position of CIV differs in the three respirasomes,
    of which only one contains the supercomplex-associated factor SCAF1, whose involvement
    in respirasome formation has long been contended. Our structures confirm that
    the ‘canonical’ respirasome (the C-respirasome, CICIII2CIV) does not contain SCAF1,
    which is instead associated to a different respirasome (the CS-respirasome), containing
    a second copy of CIV. We also identify an alternative respirasome (A-respirasome),
    with CIV bound to the ‘back’ of CI, instead of the ‘toe’. This structural characterization
    of mouse mitochondrial supercomplexes allows us to hypothesize a mechanistic basis
    for their specific role in different metabolic conditions.
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: PreCl
- _id: ScienComp
acknowledgement: Supercomplexes of the respiratory chain are established constituents
  of the oxidative phosphorylation system, but their role in mammalian metabolism
  has been hotly debated. Although recent studies have shown that different tissues/organs
  are equipped with specific sets of supercomplexes, depending on their metabolic
  needs, the notion that supercomplexes have a role in the regulation of metabolism
  has been challenged. However, irrespective of the mechanistic conclusions, the composition
  of various high molecular weight supercomplexes remains uncertain. Here, using cryogenic
  electron microscopy, we demonstrate that mammalian (mouse) tissues contain three
  defined types of ‘respirasome’, supercomplexes made of CI, CIII2 and CIV. The stoichiometry
  and position of CIV differs in the three respirasomes, of which only one contains
  the supercomplex-associated factor SCAF1, whose involvement in respirasome formation
  has long been contended. Our structures confirm that the ‘canonical’ respirasome
  (the C-respirasome, CICIII2CIV) does not contain SCAF1, which is instead associated
  to a different respirasome (the CS-respirasome), containing a second copy of CIV.
  We also identify an alternative respirasome (A-respirasome), with CIV bound to the
  ‘back’ of CI, instead of the ‘toe’. This structural characterization of mouse mitochondrial
  supercomplexes allows us to hypothesize a mechanistic basis for their specific role
  in different metabolic conditions.
article_processing_charge: No
article_type: original
author:
- first_name: Irene
  full_name: Vercellino, Irene
  id: 3ED6AF16-F248-11E8-B48F-1D18A9856A87
  last_name: Vercellino
  orcid: 0000-0001-5618-3449
- 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: Vercellino I, Sazanov LA. SCAF1 drives the compositional diversity of mammalian
    respirasomes. <i>Nature Structural and Molecular Biology</i>. 2024;31:1061-1071.
    doi:<a href="https://doi.org/10.1038/s41594-024-01255-0">10.1038/s41594-024-01255-0</a>
  apa: Vercellino, I., &#38; Sazanov, L. A. (2024). SCAF1 drives the compositional
    diversity of mammalian respirasomes. <i>Nature Structural and Molecular Biology</i>.
    Springer Nature. <a href="https://doi.org/10.1038/s41594-024-01255-0">https://doi.org/10.1038/s41594-024-01255-0</a>
  chicago: Vercellino, Irene, and Leonid A Sazanov. “SCAF1 Drives the Compositional
    Diversity of Mammalian Respirasomes.” <i>Nature Structural and Molecular Biology</i>.
    Springer Nature, 2024. <a href="https://doi.org/10.1038/s41594-024-01255-0">https://doi.org/10.1038/s41594-024-01255-0</a>.
  ieee: I. Vercellino and L. A. Sazanov, “SCAF1 drives the compositional diversity
    of mammalian respirasomes,” <i>Nature Structural and Molecular Biology</i>, vol.
    31. Springer Nature, pp. 1061–1071, 2024.
  ista: Vercellino I, Sazanov LA. 2024. SCAF1 drives the compositional diversity of
    mammalian respirasomes. Nature Structural and Molecular Biology. 31, 1061–1071.
  mla: Vercellino, Irene, and Leonid A. Sazanov. “SCAF1 Drives the Compositional Diversity
    of Mammalian Respirasomes.” <i>Nature Structural and Molecular Biology</i>, vol.
    31, Springer Nature, 2024, pp. 1061–71, doi:<a href="https://doi.org/10.1038/s41594-024-01255-0">10.1038/s41594-024-01255-0</a>.
  short: I. Vercellino, L.A. Sazanov, Nature Structural and Molecular Biology 31 (2024)
    1061–1071.
corr_author: '1'
date_created: 2024-04-14T22:01:03Z
date_published: 2024-07-01T00:00:00Z
date_updated: 2025-11-24T08:35:04Z
day: '01'
ddc:
- '572'
department:
- _id: LeSa
doi: 10.1038/s41594-024-01255-0
ec_funded: 1
external_id:
  isi:
  - '001196897300001'
  pmid:
  - '38575788'
file:
- access_level: open_access
  checksum: 21f05d188762acd7f49a97f3d09c8d9f
  content_type: application/pdf
  creator: lsazanov
  date_created: 2024-05-14T11:57:56Z
  date_updated: 2025-01-01T23:30:03Z
  embargo: 2025-01-01
  file_id: '15392'
  file_name: megacomplex_submit_NSMB_withFigures.pdf
  file_size: 24424729
  relation: main_file
file_date_updated: 2025-01-01T23:30:03Z
fulldoi: https://doi.org/10.1038/s41594-024-01255-0
has_accepted_license: '1'
intvolume: '        31'
isi: 1
language:
- iso: eng
month: '07'
oa: 1
oa_version: Submitted Version
page: 1061-1071
pmid: 1
project:
- _id: 627abdeb-2b32-11ec-9570-ec31a97243d3
  call_identifier: H2020
  grant_number: '101020697'
  name: Structure and mechanism of respiratory chain molecular machines
publication: Nature Structural and Molecular Biology
publication_identifier:
  eissn:
  - 1545-9985
  issn:
  - 1545-9993
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
  link:
  - relation: erratum
    url: https://doi.org/10.1038/s41594-025-01721-3
scopus_import: '1'
status: public
title: SCAF1 drives the compositional diversity of mammalian respirasomes
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: 31
year: '2024'
...
---
_id: '15149'
abstract:
- lang: eng
  text: The genomic binding sites of the transcription factor (TF) and tumor suppressor
    p53 are unusually diverse with regard to their chromatin features, including histone
    modifications, raising the possibility that the local chromatin environment can
    contextualize p53 regulation. Here, we show that epigenetic characteristics of
    closed chromatin, such as DNA methylation, do not influence the binding of p53
    across the genome. Instead, the ability of p53 to open chromatin and activate
    its target genes is locally restricted by its cofactor Trim24. Trim24 binds to
    both p53 and unmethylated histone 3 lysine 4 (H3K4), thereby preferentially localizing
    to those p53 sites that reside in closed chromatin, whereas it is deterred from
    accessible chromatin by H3K4 methylation. The presence of Trim24 increases cell
    viability upon stress and enables p53 to affect gene expression as a function
    of the local chromatin state. These findings link H3K4 methylation to p53 function
    and illustrate how specificity in chromatin can be achieved, not by TF-intrinsic
    sensitivity to histone modifications, but by employing chromatin-sensitive cofactors
    that locally modulate TF function.
article_processing_charge: No
article_type: original
author:
- first_name: Luke
  full_name: Isbel, Luke
  last_name: Isbel
- first_name: Murat
  full_name: Iskar, Murat
  last_name: Iskar
- first_name: Sevi
  full_name: Durdu, Sevi
  last_name: Durdu
- first_name: Joscha
  full_name: Weiss, Joscha
  last_name: Weiss
- first_name: Ralph S.
  full_name: Grand, Ralph S.
  last_name: Grand
- first_name: Eric
  full_name: Hietter-Pfeiffer, Eric
  last_name: Hietter-Pfeiffer
- first_name: Zuzanna
  full_name: Kozicka, Zuzanna
  last_name: Kozicka
- 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: Burger, Lukas
  last_name: Burger
- first_name: Nicolas H.
  full_name: Thomä, Nicolas H.
  last_name: Thomä
- first_name: Dirk
  full_name: Schübeler, Dirk
  last_name: Schübeler
citation:
  ama: Isbel L, Iskar M, Durdu S, et al. Readout of histone methylation by Trim24
    locally restricts chromatin opening by p53. <i>Nature Structural &#38; Molecular
    Biology</i>. 2023;30(7):948-957. doi:<a href="https://doi.org/10.1038/s41594-023-01021-8">10.1038/s41594-023-01021-8</a>
  apa: Isbel, L., Iskar, M., Durdu, S., Weiss, J., Grand, R. S., Hietter-Pfeiffer,
    E., … Schübeler, D. (2023). Readout of histone methylation by Trim24 locally restricts
    chromatin opening by p53. <i>Nature Structural &#38; Molecular Biology</i>. Springer
    Nature. <a href="https://doi.org/10.1038/s41594-023-01021-8">https://doi.org/10.1038/s41594-023-01021-8</a>
  chicago: Isbel, Luke, Murat Iskar, Sevi Durdu, Joscha Weiss, Ralph S. Grand, Eric
    Hietter-Pfeiffer, Zuzanna Kozicka, et al. “Readout of Histone Methylation by Trim24
    Locally Restricts Chromatin Opening by P53.” <i>Nature Structural &#38; Molecular
    Biology</i>. Springer Nature, 2023. <a href="https://doi.org/10.1038/s41594-023-01021-8">https://doi.org/10.1038/s41594-023-01021-8</a>.
  ieee: L. Isbel <i>et al.</i>, “Readout of histone methylation by Trim24 locally
    restricts chromatin opening by p53,” <i>Nature Structural &#38; Molecular Biology</i>,
    vol. 30, no. 7. Springer Nature, pp. 948–957, 2023.
  ista: Isbel L, Iskar M, Durdu S, Weiss J, Grand RS, Hietter-Pfeiffer E, Kozicka
    Z, Michael AK, Burger L, Thomä NH, Schübeler D. 2023. Readout of histone methylation
    by Trim24 locally restricts chromatin opening by p53. Nature Structural &#38;
    Molecular Biology. 30(7), 948–957.
  mla: Isbel, Luke, et al. “Readout of Histone Methylation by Trim24 Locally Restricts
    Chromatin Opening by P53.” <i>Nature Structural &#38; Molecular Biology</i>, vol.
    30, no. 7, Springer Nature, 2023, pp. 948–57, doi:<a href="https://doi.org/10.1038/s41594-023-01021-8">10.1038/s41594-023-01021-8</a>.
  short: L. Isbel, M. Iskar, S. Durdu, J. Weiss, R.S. Grand, E. Hietter-Pfeiffer,
    Z. Kozicka, A.K. Michael, L. Burger, N.H. Thomä, D. Schübeler, Nature Structural
    &#38; Molecular Biology 30 (2023) 948–957.
date_created: 2024-03-21T07:53:24Z
date_published: 2023-06-29T00:00:00Z
date_updated: 2024-03-25T12:37:20Z
day: '29'
doi: 10.1038/s41594-023-01021-8
extern: '1'
external_id:
  pmid:
  - '37386214'
fulldoi: https://doi.org/10.1038/s41594-023-01021-8
intvolume: '        30'
issue: '7'
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1038/s41594-023-01021-8
month: '06'
oa: 1
oa_version: Published Version
page: 948-957
pmid: 1
publication: Nature Structural & Molecular Biology
publication_identifier:
  eissn:
  - 1545-9985
  issn:
  - 1545-9993
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Readout of histone methylation by Trim24 locally restricts chromatin opening
  by p53
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 30
year: '2023'
...
---
_id: '12262'
abstract:
- lang: eng
  text: The AAA-ATPase Drg1 is a key factor in eukaryotic ribosome biogenesis that
    initiates cytoplasmic maturation of the large ribosomal subunit. Drg1 releases
    the shuttling maturation factor Rlp24 from pre-60S particles shortly after nuclear
    export, a strict requirement for downstream maturation. The molecular mechanism
    of release remained elusive. Here, we report a series of cryo-EM structures that
    captured the extraction of Rlp24 from pre-60S particles by Saccharomyces cerevisiae
    Drg1. These structures reveal that Arx1 and the eukaryote-specific rRNA expansion
    segment ES27 form a joint docking platform that positions Drg1 for efficient extraction
    of Rlp24 from the pre-ribosome. The tips of the Drg1 N domains thereby guide the
    Rlp24 C terminus into the central pore of the Drg1 hexamer, enabling extraction
    by a hand-over-hand translocation mechanism. Our results uncover substrate recognition
    and processing by Drg1 step by step and provide a comprehensive mechanistic picture
    of the conserved modus operandi of AAA-ATPases.
acknowledged_ssus:
- _id: EM-Fac
acknowledgement: "We thank M. Fromont-Racine, A. Johnson, J. Woolford, S. Rospert,
  J. P. G. Ballesta and\r\nE. Hurt for supplying antibodies. The work was supported
  by Boehringer Ingelheim (to\r\nD. H.), the Austrian Science Foundation FWF (grants
  32536 and 32977 to H. B.), the\r\nUK Medical Research Council (MR/T012412/1 to A.
  J. W.) and the German Research\r\nFoundation (Emmy Noether Programme STE 2517/1-1
  and STE 2517/5-1 to F.S.). We\r\nthank Norberto Escudero-Urquijo, Pablo Castro-Hartmann
  and K. Dent, Cambridge\r\nInstitute for Medical Research, for their help in cryo-EM
  during early phases of this\r\nproject. This research was supported by the Scientific
  Service Units of IST Austria through\r\nresources provided by the Electron Microscopy
  Facility. We thank S. Keller, Institute of\r\nMolecular Biosciences (Biophysics),
  University Graz for support with the quantification of\r\nthe SPR particle release
  assay. We thank I. Schaffner, University of Natural Resources and\r\nLife Sciences,
  Vienna for her help in early stages of the SPR experiments."
article_processing_charge: No
article_type: original
author:
- first_name: Michael
  full_name: Prattes, Michael
  last_name: Prattes
- first_name: Irina
  full_name: Grishkovskaya, Irina
  last_name: Grishkovskaya
- first_name: Victor-Valentin
  full_name: Hodirnau, Victor-Valentin
  id: 3661B498-F248-11E8-B48F-1D18A9856A87
  last_name: Hodirnau
- first_name: Christina
  full_name: Hetzmannseder, Christina
  last_name: Hetzmannseder
- first_name: Gertrude
  full_name: Zisser, Gertrude
  last_name: Zisser
- first_name: Carolin
  full_name: Sailer, Carolin
  last_name: Sailer
- first_name: Vasileios
  full_name: Kargas, Vasileios
  last_name: Kargas
- first_name: Mathias
  full_name: Loibl, Mathias
  last_name: Loibl
- first_name: Magdalena
  full_name: Gerhalter, Magdalena
  last_name: Gerhalter
- first_name: Lisa
  full_name: Kofler, Lisa
  last_name: Kofler
- first_name: Alan J.
  full_name: Warren, Alan J.
  last_name: Warren
- first_name: Florian
  full_name: Stengel, Florian
  last_name: Stengel
- first_name: David
  full_name: Haselbach, David
  last_name: Haselbach
- first_name: Helmut
  full_name: Bergler, Helmut
  last_name: Bergler
citation:
  ama: Prattes M, Grishkovskaya I, Hodirnau V-V, et al. Visualizing maturation factor
    extraction from the nascent ribosome by the AAA-ATPase Drg1. <i>Nature Structural
    &#38; Molecular Biology</i>. 2022;29(9):942-953. doi:<a href="https://doi.org/10.1038/s41594-022-00832-5">10.1038/s41594-022-00832-5</a>
  apa: Prattes, M., Grishkovskaya, I., Hodirnau, V.-V., Hetzmannseder, C., Zisser,
    G., Sailer, C., … Bergler, H. (2022). Visualizing maturation factor extraction
    from the nascent ribosome by the AAA-ATPase Drg1. <i>Nature Structural &#38; Molecular
    Biology</i>. Springer Nature. <a href="https://doi.org/10.1038/s41594-022-00832-5">https://doi.org/10.1038/s41594-022-00832-5</a>
  chicago: Prattes, Michael, Irina Grishkovskaya, Victor-Valentin Hodirnau, Christina
    Hetzmannseder, Gertrude Zisser, Carolin Sailer, Vasileios Kargas, et al. “Visualizing
    Maturation Factor Extraction from the Nascent Ribosome by the AAA-ATPase Drg1.”
    <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2022. <a href="https://doi.org/10.1038/s41594-022-00832-5">https://doi.org/10.1038/s41594-022-00832-5</a>.
  ieee: M. Prattes <i>et al.</i>, “Visualizing maturation factor extraction from the
    nascent ribosome by the AAA-ATPase Drg1,” <i>Nature Structural &#38; Molecular
    Biology</i>, vol. 29, no. 9. Springer Nature, pp. 942–953, 2022.
  ista: Prattes M, Grishkovskaya I, Hodirnau V-V, Hetzmannseder C, Zisser G, Sailer
    C, Kargas V, Loibl M, Gerhalter M, Kofler L, Warren AJ, Stengel F, Haselbach D,
    Bergler H. 2022. Visualizing maturation factor extraction from the nascent ribosome
    by the AAA-ATPase Drg1. Nature Structural &#38; Molecular Biology. 29(9), 942–953.
  mla: Prattes, Michael, et al. “Visualizing Maturation Factor Extraction from the
    Nascent Ribosome by the AAA-ATPase Drg1.” <i>Nature Structural &#38; Molecular
    Biology</i>, vol. 29, no. 9, Springer Nature, 2022, pp. 942–53, doi:<a href="https://doi.org/10.1038/s41594-022-00832-5">10.1038/s41594-022-00832-5</a>.
  short: M. Prattes, I. Grishkovskaya, V.-V. Hodirnau, C. Hetzmannseder, G. Zisser,
    C. Sailer, V. Kargas, M. Loibl, M. Gerhalter, L. Kofler, A.J. Warren, F. Stengel,
    D. Haselbach, H. Bergler, Nature Structural &#38; Molecular Biology 29 (2022)
    942–953.
date_created: 2023-01-16T09:59:06Z
date_published: 2022-09-12T00:00:00Z
date_updated: 2023-08-04T09:52:20Z
day: '12'
ddc:
- '570'
department:
- _id: EM-Fac
doi: 10.1038/s41594-022-00832-5
external_id:
  isi:
  - '000852942100004'
  pmid:
  - '36097293'
file:
- access_level: open_access
  checksum: 2d5c3ec01718fefd7553052b0b8a0793
  content_type: application/pdf
  creator: dernst
  date_created: 2023-01-30T10:00:04Z
  date_updated: 2023-01-30T10:00:04Z
  file_id: '12447'
  file_name: 2022_NatureStrucMolecBio_Prattes.pdf
  file_size: 9935057
  relation: main_file
  success: 1
file_date_updated: 2023-01-30T10:00:04Z
fulldoi: https://doi.org/10.1038/s41594-022-00832-5
has_accepted_license: '1'
intvolume: '        29'
isi: 1
issue: '9'
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
page: 942-953
pmid: 1
publication: Nature Structural & Molecular Biology
publication_identifier:
  eissn:
  - 1545-9985
  issn:
  - 1545-9993
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Visualizing maturation factor extraction from the nascent ribosome by the AAA-ATPase
  Drg1
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: 29
year: '2022'
...
---
_id: '15131'
abstract:
- lang: eng
  text: RNA modifications are widespread in biology and abundant in ribosomal RNA.
    However, the importance of these modifications is not well understood. We show
    that methylation of a single nucleotide, in the catalytic center of the large
    subunit, gates ribosome assembly. Massively parallel mutational scanning of the
    essential nuclear GTPase Nog2 identified important interactions with rRNA, particularly
    with the 2′-<jats:italic>O</jats:italic>-methylated A-site base Gm2922. We found
    that methylation of G2922 is needed for assembly and efficient nuclear export
    of the large subunit. Critically, we identified single amino acid changes in Nog2
    that completely bypass dependence on G2922 methylation and used cryoelectron microscopy
    to directly visualize how methylation flips Gm2922 into the active site channel
    of Nog2. This work demonstrates that a single RNA modification is a critical checkpoint
    in ribosome biogenesis, suggesting that such modifications can play an important
    role in regulation and assembly of macromolecular machines.
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: James N.
  full_name: Yelland, James N.
  last_name: Yelland
- 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: Joshua J.
  full_name: Black, Joshua J.
  last_name: Black
- first_name: David W.
  full_name: Taylor, David W.
  last_name: Taylor
- first_name: Arlen W.
  full_name: Johnson, Arlen W.
  last_name: Johnson
citation:
  ama: Yelland JN, Bravo JPK, Black JJ, Taylor DW, Johnson AW. A single 2′-O-methylation
    of ribosomal RNA gates assembly of a functional ribosome. <i>Nature Structural
    &#38; Molecular Biology</i>. 2022;30:91-98. doi:<a href="https://doi.org/10.1038/s41594-022-00891-8">10.1038/s41594-022-00891-8</a>
  apa: Yelland, J. N., Bravo, J. P. K., Black, J. J., Taylor, D. W., &#38; Johnson,
    A. W. (2022). A single 2′-O-methylation of ribosomal RNA gates assembly of a functional
    ribosome. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a
    href="https://doi.org/10.1038/s41594-022-00891-8">https://doi.org/10.1038/s41594-022-00891-8</a>
  chicago: Yelland, James N., Jack Peter Kelly Bravo, Joshua J. Black, David W. Taylor,
    and Arlen W. Johnson. “A Single 2′-O-Methylation of Ribosomal RNA Gates Assembly
    of a Functional Ribosome.” <i>Nature Structural &#38; Molecular Biology</i>. Springer
    Nature, 2022. <a href="https://doi.org/10.1038/s41594-022-00891-8">https://doi.org/10.1038/s41594-022-00891-8</a>.
  ieee: J. N. Yelland, J. P. K. Bravo, J. J. Black, D. W. Taylor, and A. W. Johnson,
    “A single 2′-O-methylation of ribosomal RNA gates assembly of a functional ribosome,”
    <i>Nature Structural &#38; Molecular Biology</i>, vol. 30. Springer Nature, pp.
    91–98, 2022.
  ista: Yelland JN, Bravo JPK, Black JJ, Taylor DW, Johnson AW. 2022. A single 2′-O-methylation
    of ribosomal RNA gates assembly of a functional ribosome. Nature Structural &#38;
    Molecular Biology. 30, 91–98.
  mla: Yelland, James N., et al. “A Single 2′-O-Methylation of Ribosomal RNA Gates
    Assembly of a Functional Ribosome.” <i>Nature Structural &#38; Molecular Biology</i>,
    vol. 30, Springer Nature, 2022, pp. 91–98, doi:<a href="https://doi.org/10.1038/s41594-022-00891-8">10.1038/s41594-022-00891-8</a>.
  short: J.N. Yelland, J.P.K. Bravo, J.J. Black, D.W. Taylor, A.W. Johnson, Nature
    Structural &#38; Molecular Biology 30 (2022) 91–98.
date_created: 2024-03-20T10:41:45Z
date_published: 2022-12-19T00:00:00Z
date_updated: 2024-06-04T06:27:09Z
day: '19'
doi: 10.1038/s41594-022-00891-8
extern: '1'
external_id:
  pmid:
  - '36536102'
fulldoi: https://doi.org/10.1038/s41594-022-00891-8
intvolume: '        30'
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1038/s41594-022-00891-8
month: '12'
oa: 1
oa_version: Published Version
page: 91-98
pmid: 1
publication: Nature Structural & Molecular Biology
publication_identifier:
  eissn:
  - 1545-9985
  issn:
  - 1545-9993
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: A single 2′-O-methylation of ribosomal RNA gates assembly of a functional ribosome
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 30
year: '2022'
...
---
_id: '8581'
abstract:
- lang: eng
  text: The majority of adenosine triphosphate (ATP) powering cellular processes in
    eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present
    the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo,
    determined by cryo-electron microscopy. Subunits in the membrane domain are arranged
    in the ‘proton translocation cluster’ attached to the c-ring and a more distant
    ‘hook apparatus’ holding subunit e. Unexpectedly, this subunit is anchored to
    a lipid ‘plug’ capping the c-ring. We present a detailed proton translocation
    pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM
    maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled
    c-ring, suggesting permeability transition pore opening. We propose a model for
    the permeability transition pore opening, whereby subunit e pulls the lipid plug
    out of the c-ring. Our structure will allow the design of drugs for many emerging
    applications in medicine.
acknowledged_ssus:
- _id: EM-Fac
- _id: ScienComp
acknowledgement: We thank J. Novacek from CEITEC (Brno, Czech Republic) for assistance
  with collecting the FEI Krios dataset and iNEXT for providing access to CEITEC.
  We thank the IST Austria EM facility for access and assistance with collecting the
  FEI Glacios dataset. Data processing was performed at the IST high-performance computing
  cluster. This work has been supported by iNEXT EM HEDC (proposal 4506), funded by
  the Horizon 2020 Programme of the European Commission.
article_processing_charge: No
article_type: original
author:
- first_name: Gergely
  full_name: Pinke, Gergely
  id: 4D5303E6-F248-11E8-B48F-1D18A9856A87
  last_name: Pinke
- first_name: Long
  full_name: Zhou, Long
  id: 3E751364-F248-11E8-B48F-1D18A9856A87
  last_name: Zhou
  orcid: 0000-0002-1864-8951
- 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: Pinke G, Zhou L, Sazanov LA. Cryo-EM structure of the entire mammalian F-type
    ATP synthase. <i>Nature Structural and Molecular Biology</i>. 2020;27(11):1077-1085.
    doi:<a href="https://doi.org/10.1038/s41594-020-0503-8">10.1038/s41594-020-0503-8</a>
  apa: Pinke, G., Zhou, L., &#38; Sazanov, L. A. (2020). Cryo-EM structure of the
    entire mammalian F-type ATP synthase. <i>Nature Structural and Molecular Biology</i>.
    Springer Nature. <a href="https://doi.org/10.1038/s41594-020-0503-8">https://doi.org/10.1038/s41594-020-0503-8</a>
  chicago: Pinke, Gergely, Long Zhou, and Leonid A Sazanov. “Cryo-EM Structure of
    the Entire Mammalian F-Type ATP Synthase.” <i>Nature Structural and Molecular
    Biology</i>. Springer Nature, 2020. <a href="https://doi.org/10.1038/s41594-020-0503-8">https://doi.org/10.1038/s41594-020-0503-8</a>.
  ieee: G. Pinke, L. Zhou, and L. A. Sazanov, “Cryo-EM structure of the entire mammalian
    F-type ATP synthase,” <i>Nature Structural and Molecular Biology</i>, vol. 27,
    no. 11. Springer Nature, pp. 1077–1085, 2020.
  ista: Pinke G, Zhou L, Sazanov LA. 2020. Cryo-EM structure of the entire mammalian
    F-type ATP synthase. Nature Structural and Molecular Biology. 27(11), 1077–1085.
  mla: Pinke, Gergely, et al. “Cryo-EM Structure of the Entire Mammalian F-Type ATP
    Synthase.” <i>Nature Structural and Molecular Biology</i>, vol. 27, no. 11, Springer
    Nature, 2020, pp. 1077–85, doi:<a href="https://doi.org/10.1038/s41594-020-0503-8">10.1038/s41594-020-0503-8</a>.
  short: G. Pinke, L. Zhou, L.A. Sazanov, Nature Structural and Molecular Biology
    27 (2020) 1077–1085.
date_created: 2020-09-28T08:59:27Z
date_published: 2020-11-01T00:00:00Z
date_updated: 2025-07-10T11:57:09Z
day: '01'
department:
- _id: LeSa
doi: 10.1038/s41594-020-0503-8
external_id:
  isi:
  - '000569299400004'
  pmid:
  - '32929284'
fulldoi: https://doi.org/10.1038/s41594-020-0503-8
intvolume: '        27'
isi: 1
issue: '11'
language:
- iso: eng
month: '11'
oa_version: None
page: 1077-1085
pmid: 1
publication: Nature Structural and Molecular Biology
publication_identifier:
  eissn:
  - 1545-9985
  issn:
  - 1545-9993
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
  link:
  - description: News on IST Homepage
    relation: press_release
    url: https://ist.ac.at/en/news/structure-of-atpase-solved/
scopus_import: '1'
status: public
title: Cryo-EM structure of the entire mammalian F-type ATP synthase
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 27
year: '2020'
...
---
_id: '8438'
article_processing_charge: No
article_type: letter_note
author:
- first_name: Vilius
  full_name: Kurauskas, Vilius
  last_name: Kurauskas
- first_name: Audrey
  full_name: Hessel, Audrey
  last_name: Hessel
- first_name: François
  full_name: Dehez, François
  last_name: Dehez
- first_name: Christophe
  full_name: Chipot, Christophe
  last_name: Chipot
- first_name: Beate
  full_name: Bersch, Beate
  last_name: Bersch
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. Dynamics and
    interactions of AAC3 in DPC are not functionally relevant. <i>Nature Structural
    &#38; Molecular Biology</i>. 2018;25(9):745-747. doi:<a href="https://doi.org/10.1038/s41594-018-0127-4">10.1038/s41594-018-0127-4</a>
  apa: Kurauskas, V., Hessel, A., Dehez, F., Chipot, C., Bersch, B., &#38; Schanda,
    P. (2018). Dynamics and interactions of AAC3 in DPC are not functionally relevant.
    <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href="https://doi.org/10.1038/s41594-018-0127-4">https://doi.org/10.1038/s41594-018-0127-4</a>
  chicago: Kurauskas, Vilius, Audrey Hessel, François Dehez, Christophe Chipot, Beate
    Bersch, and Paul Schanda. “Dynamics and Interactions of AAC3 in DPC Are Not Functionally
    Relevant.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature,
    2018. <a href="https://doi.org/10.1038/s41594-018-0127-4">https://doi.org/10.1038/s41594-018-0127-4</a>.
  ieee: V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, and P. Schanda, “Dynamics
    and interactions of AAC3 in DPC are not functionally relevant,” <i>Nature Structural
    &#38; Molecular Biology</i>, vol. 25, no. 9. Springer Nature, pp. 745–747, 2018.
  ista: Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. 2018. Dynamics
    and interactions of AAC3 in DPC are not functionally relevant. Nature Structural
    &#38; Molecular Biology. 25(9), 745–747.
  mla: Kurauskas, Vilius, et al. “Dynamics and Interactions of AAC3 in DPC Are Not
    Functionally Relevant.” <i>Nature Structural &#38; Molecular Biology</i>, vol.
    25, no. 9, Springer Nature, 2018, pp. 745–47, doi:<a href="https://doi.org/10.1038/s41594-018-0127-4">10.1038/s41594-018-0127-4</a>.
  short: V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, P. Schanda, Nature
    Structural &#38; Molecular Biology 25 (2018) 745–747.
date_created: 2020-09-18T10:04:59Z
date_published: 2018-09-03T00:00:00Z
date_updated: 2021-01-12T08:19:16Z
day: '03'
doi: 10.1038/s41594-018-0127-4
extern: '1'
fulldoi: https://doi.org/10.1038/s41594-018-0127-4
intvolume: '        25'
issue: '9'
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
month: '09'
oa_version: None
page: 745-747
publication: Nature Structural & Molecular Biology
publication_identifier:
  issn:
  - 1545-9993
  - 1545-9985
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Dynamics and interactions of AAC3 in DPC are not functionally relevant
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 25
year: '2018'
...
---
_id: '515'
abstract:
- lang: eng
  text: 'The oxidative phosphorylation electron transport chain (OXPHOS-ETC) of the
    inner mitochondrial membrane is composed of five large protein complexes, named
    CI-CV. These complexes convert energy from the food we eat into ATP, a small molecule
    used to power a multitude of essential reactions throughout the cell. OXPHOS-ETC
    complexes are organized into supercomplexes (SCs) of defined stoichiometry: CI
    forms a supercomplex with CIII2 and CIV (SC I+III2+IV, known as the respirasome),
    as well as with CIII2 alone (SC I+III2). CIII2 forms a supercomplex with CIV (SC
    III2+IV) and CV forms dimers (CV2). Recent cryo-EM studies have revealed the structures
    of SC I+III2+IV and SC I+III2. Furthermore, recent work has shed light on the
    assembly and function of the SCs. Here we review and compare these recent studies
    and discuss how they have advanced our understanding of mitochondrial electron
    transport.'
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: 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, Sazanov LA. Clarifying the supercomplex: The higher-order organization
    of the mitochondrial electron transport chain. <i>Nature Structural and Molecular
    Biology</i>. 2017;24(10):800-808. doi:<a href="https://doi.org/10.1038/nsmb.3460">10.1038/nsmb.3460</a>'
  apa: 'Letts, J. A., &#38; Sazanov, L. A. (2017). Clarifying the supercomplex: The
    higher-order organization of the mitochondrial electron transport chain. <i>Nature
    Structural and Molecular Biology</i>. Nature Publishing Group. <a href="https://doi.org/10.1038/nsmb.3460">https://doi.org/10.1038/nsmb.3460</a>'
  chicago: 'Letts, James A, and Leonid A Sazanov. “Clarifying the Supercomplex: The
    Higher-Order Organization of the Mitochondrial Electron Transport Chain.” <i>Nature
    Structural and Molecular Biology</i>. Nature Publishing Group, 2017. <a href="https://doi.org/10.1038/nsmb.3460">https://doi.org/10.1038/nsmb.3460</a>.'
  ieee: 'J. A. Letts and L. A. Sazanov, “Clarifying the supercomplex: The higher-order
    organization of the mitochondrial electron transport chain,” <i>Nature Structural
    and Molecular Biology</i>, vol. 24, no. 10. Nature Publishing Group, pp. 800–808,
    2017.'
  ista: 'Letts JA, Sazanov LA. 2017. Clarifying the supercomplex: The higher-order
    organization of the mitochondrial electron transport chain. Nature Structural
    and Molecular Biology. 24(10), 800–808.'
  mla: 'Letts, James A., and Leonid A. Sazanov. “Clarifying the Supercomplex: The
    Higher-Order Organization of the Mitochondrial Electron Transport Chain.” <i>Nature
    Structural and Molecular Biology</i>, vol. 24, no. 10, Nature Publishing Group,
    2017, pp. 800–08, doi:<a href="https://doi.org/10.1038/nsmb.3460">10.1038/nsmb.3460</a>.'
  short: J.A. Letts, L.A. Sazanov, Nature Structural and Molecular Biology 24 (2017)
    800–808.
corr_author: '1'
date_created: 2018-12-11T11:46:54Z
date_published: 2017-10-05T00:00:00Z
date_updated: 2025-09-18T09:47:41Z
day: '05'
ddc:
- '572'
department:
- _id: LeSa
doi: 10.1038/nsmb.3460
ec_funded: 1
external_id:
  isi:
  - '000412278000006'
file:
- access_level: open_access
  checksum: 9bc7e8c41b43636dd7566289e511f096
  content_type: application/pdf
  creator: lsazanov
  date_created: 2019-11-07T12:51:07Z
  date_updated: 2020-07-14T12:46:36Z
  file_id: '6993'
  file_name: 29893_2_merged_1501257589_red.pdf
  file_size: 4118385
  relation: main_file
file_date_updated: 2020-07-14T12:46:36Z
fulldoi: https://doi.org/10.1038/nsmb.3460
has_accepted_license: '1'
intvolume: '        24'
isi: 1
issue: '10'
language:
- iso: eng
month: '10'
oa: 1
oa_version: Submitted Version
page: 800 - 808
project:
- _id: 2590DB08-B435-11E9-9278-68D0E5697425
  call_identifier: H2020
  grant_number: '701309'
  name: Atomic Resolution Structures of Mitochondrial Respiratory Chain Supercomplexes
publication: Nature Structural and Molecular Biology
publication_identifier:
  issn:
  - 1545-9993
publication_status: published
publisher: Nature Publishing Group
publist_id: '7304'
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Clarifying the supercomplex: The higher-order organization of the mitochondrial
  electron transport chain'
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 24
year: '2017'
...
---
OA_type: closed access
_id: '3141'
abstract:
- lang: eng
  text: The two actin-related subunits of the Arp2/3 complex, Arp2 and Arp3, are proposed
    to form a pseudo actin dimer that nucleates actin polymerization. However, in
    the crystal structure of the inactive complex, they are too far apart to form
    such a nucleus. Here, we show using EM that yeast and bovine Arp2/3 complexes
    exist in a distribution among open, intermediate and closed conformations. The
    crystal structure docks well into the open conformation. The activator WASp binds
    at the cleft between Arp2 and Arp3, and all WASp-bound complexes are closed. The
    inhibitor coronin binds near the p35 subunit, and all coronin-bound complexes
    are open. Activating and loss-of-function mutations in the p35 subunit skew conformational
    distribution in opposite directions, closed and open, respectively. We conclude
    that WASp stabilizes p35-dependent closure of the complex, holding Arp2 and Arp3
    closer together to nucleate an actin filament.
article_processing_charge: No
article_type: original
author:
- first_name: Avital
  full_name: Rodal, Avital
  last_name: Rodal
- first_name: Olga
  full_name: Sokolova, Olga
  last_name: Sokolova
- first_name: Deborah
  full_name: Robins, Deborah
  last_name: Robins
- first_name: Karen
  full_name: Daugherty, Karen
  last_name: Daugherty
- first_name: Simon
  full_name: Hippenmeyer, Simon
  id: 37B36620-F248-11E8-B48F-1D18A9856A87
  last_name: Hippenmeyer
  orcid: 0000-0003-2279-1061
- first_name: Howard
  full_name: Riezman, Howard
  last_name: Riezman
- first_name: Nikolaus
  full_name: Grigorieff, Nikolaus
  last_name: Grigorieff
- first_name: Bruce
  full_name: Goode, Bruce
  last_name: Goode
citation:
  ama: Rodal A, Sokolova O, Robins D, et al. Conformational changes in the Arp2 3
    complex leading to actin nucleation. <i>Nature Structural and Molecular Biology</i>.
    2004;12(1):26-31. doi:<a href="https://doi.org/10.1038/nsmb870">10.1038/nsmb870</a>
  apa: Rodal, A., Sokolova, O., Robins, D., Daugherty, K., Hippenmeyer, S., Riezman,
    H., … Goode, B. (2004). Conformational changes in the Arp2 3 complex leading to
    actin nucleation. <i>Nature Structural and Molecular Biology</i>. Nature Publishing
    Group. <a href="https://doi.org/10.1038/nsmb870">https://doi.org/10.1038/nsmb870</a>
  chicago: Rodal, Avital, Olga Sokolova, Deborah Robins, Karen Daugherty, Simon Hippenmeyer,
    Howard Riezman, Nikolaus Grigorieff, and Bruce Goode. “Conformational Changes
    in the Arp2 3 Complex Leading to Actin Nucleation.” <i>Nature Structural and Molecular
    Biology</i>. Nature Publishing Group, 2004. <a href="https://doi.org/10.1038/nsmb870">https://doi.org/10.1038/nsmb870</a>.
  ieee: A. Rodal <i>et al.</i>, “Conformational changes in the Arp2 3 complex leading
    to actin nucleation,” <i>Nature Structural and Molecular Biology</i>, vol. 12,
    no. 1. Nature Publishing Group, pp. 26–31, 2004.
  ista: Rodal A, Sokolova O, Robins D, Daugherty K, Hippenmeyer S, Riezman H, Grigorieff
    N, Goode B. 2004. Conformational changes in the Arp2 3 complex leading to actin
    nucleation. Nature Structural and Molecular Biology. 12(1), 26–31.
  mla: Rodal, Avital, et al. “Conformational Changes in the Arp2 3 Complex Leading
    to Actin Nucleation.” <i>Nature Structural and Molecular Biology</i>, vol. 12,
    no. 1, Nature Publishing Group, 2004, pp. 26–31, doi:<a href="https://doi.org/10.1038/nsmb870">10.1038/nsmb870</a>.
  short: A. Rodal, O. Sokolova, D. Robins, K. Daugherty, S. Hippenmeyer, H. Riezman,
    N. Grigorieff, B. Goode, Nature Structural and Molecular Biology 12 (2004) 26–31.
das_tickbox: '1'
date_created: 2018-12-11T12:01:38Z
date_published: 2004-12-12T00:00:00Z
date_updated: 2026-07-15T12:44:10Z
day: '12'
doi: 10.1038/nsmb870
extern: '1'
external_id:
  pmid:
  - '15592479'
fulldoi: https://doi.org/10.1038/nsmb870
intvolume: '        12'
issue: '1'
language:
- iso: eng
month: '12'
oa_version: None
page: 26 - 31
pmid: 1
publication: Nature Structural and Molecular Biology
publication_identifier:
  eissn:
  - 1545-9985
  issn:
  - 1545-9993
publication_status: published
publisher: Nature Publishing Group
publist_id: '3554'
status: public
title: Conformational changes in the Arp2 3 complex leading to actin nucleation
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 12
year: '2004'
...