Evidence map›Paper›PMID 24034246›Full record

ArticleCell2013

Molecular architecture of the ATP-dependent chromatin-remodeling complex SWR1.

Vu Q Nguyen, Anand Ranjan, Florian Stengel, Debbie Wei, Ruedi Aebersold, Carl Wu, Andres E Leschziner

Abstract read
In one paragraph

Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

89 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Structure of the human TIP60 complex.Nature communications · 2024
    Article
  10. Review
  11. Differential roles of putative arginine fingers of AAAbioRxiv : the preprint server for biology · 2024
    Article
  12. Article
  13. Article
  14. PMT6 Is Required for SWC4 in Positively Modulating Pepper Thermotolerance.International journal of molecular sciences · 2023
    Article
  15. Article
  16. Nodavirus RNA replication crown architecture reveals proto-crown precursor and viral protein A conformational switching.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Discovery of small-molecule inhibitors of RUVBL1/2 ATPase.Bioorganic & medicinal chemistry · 2022
    Article
  18. Article
  19. Article
  20. Article

29 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Vu Q NguyenDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
Anand Ranjan
Florian Stengel
Debbie Wei
Ruedi Aebersold
Carl Wu
Andres E Leschziner

Funding

Training in Molecular, Cellular, and Chemical BiologyT32GM007598 · NIGMS · HARVARD UNIVERSITY · PI DULAC, CATHERINE · 1985 to 2019
$16.2M
A comparative structural study of ATP-dependent chromatin remodeling complexesR01GM092895 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LESCHZINER, ANDRES · 2011 to 2021
$3.0M
European Research Council 233226Howard Hughes Medical InstituteNIGMS NIH HHS GM007598NIGMS NIH HHS R01 GM092895NIGMS NIH HHS T32 GM007598
6 · The paper itself

Abstract

The ATP-dependent chromatin-remodeling complex SWR1 exchanges a variant histone H2A.Z/H2B dimer for a canonical H2A/H2B dimer at nucleosomes flanking histone-depleted regions, such as promoters. This localization of H2A.Z is conserved throughout eukaryotes. SWR1 is a 1 megadalton complex containing 14 different polypeptides, including the AAA+ ATPases Rvb1 and Rvb2. Using electron microscopy, we obtained the three-dimensional structure of SWR1 and mapped its major functional components. Our data show that SWR1 contains a single heterohexameric Rvb1/Rvb2 ring that, together with the catalytic subunit Swr1, brackets two independently assembled multisubunit modules. We also show that SWR1 undergoes a large conformational change upon engaging a limited region of the nucleosome core particle. Our work suggests an important structural role for the Rvbs and a distinct substrate-handling mode by SWR1, thereby providing a structural framework for understanding the complex dimer-exchange reaction.

Indexed as

Chromatin Assembly and DisassemblyAdenosine TriphosphatasesDimerizationDNA HelicasesMultiprotein ComplexesNucleosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsAdenosine TriphosphatasesDNA HelicasesMultiprotein ComplexesNucleosomesRVB1 protein, S cerevisiaeRVB2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSwr1 protein, S cerevisiaeTranscription Factors

Identifiers

PMID24034246
PMCPMC3776929

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.