---
_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
- 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
- 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. 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>. Springer Nature, 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.
  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>, Springer Nature, 2024, 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 (2024).
date_created: 2024-02-12T09:59:45Z
date_published: 2024-02-05T00:00:00Z
date_updated: 2024-03-05T09:27:47Z
day: '05'
ddc:
- '570'
department:
- _id: FlSc
- _id: ScienComp
- _id: EM-Fac
doi: 10.1038/s41594-023-01201-6
external_id:
  pmid:
  - '38316877'
has_accepted_license: '1'
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1038/s41594-023-01201-6
month: '02'
oa: 1
oa_version: Published Version
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: epub_ahead
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/
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2024'
...
---
_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
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: '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'
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'
...