Evidence map›Paper›PMID 23401505›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Structure of an actin-related subcomplex of the SWI/SNF chromatin remodeler.

Heidi L Schubert, Jacqueline Wittmeyer, Margaret M Kasten, Kaede Hinata, David C Rawling, Annie Héroux, Bradley R Cairns, Christopher P Hill

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
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

65 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

5 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

8 authors at 4 institutions in 1 country.

Heidi L SchubertDepartment of Biochemistry, University of Utah, Salt Lake City, UT 84112, USA.
Jacqueline Wittmeyer
Margaret M Kasten
Kaede Hinata
David C Rawling
Annie Héroux
Bradley R Cairns
Christopher P Hill
Howard Hughes Medical Institute · USUniversity of Utah · USBrookhaven National Laboratory · USHuntsman Cancer Institute · US

Funding

ANALYSIS OF THE CHROMATIN-REMODELING COMPLEX RSCR01GM060415 · NIGMS · UNIVERSITY OF UTAH · PI CAIRNS, BRADLEY R. · 1999 to 2011
$3.1M
Nucleosome Reorganizing/Remodeling ComplexesR01GM076242 · NIGMS · UNIVERSITY OF UTAH · PI HILL, CHRISTOPHER P. · 2006 to 2013
$2.2M
Howard Hughes Medical InstituteNIGMS NIH HHS GM076242NIGMS NIH HHS GM60415NIGMS NIH HHS R01 GM060415NIGMS NIH HHS R01 GM076242
6 · The paper itself

Abstract

The packaging of DNA into nucleosomal structures limits access for templated processes such as transcription and DNA repair. The repositioning or ejection of nucleosomes is therefore critically important for regulated events, including gene expression. This activity is provided by chromatin remodeling complexes, or remodelers, which are typically large, multisubunit complexes that use an ATPase subunit to translocate the DNA. Many remodelers contain pairs or multimers of actin-related proteins (ARPs) that contact the helicase-SANT-associated (HSA) domain within the catalytic ATPase subunit and are thought to regulate ATPase activity. Here, we determined the structure of a four-protein subcomplex within the SWI/SNF remodeler that comprises the Snf2 HSA domain, Arp7, Arp9, and repressor of Ty1 transposition, gene 102 (Rtt102). Surprisingly, unlike characterized actin-actin associations, the two ARPs pack like spoons and straddle the HSA domain, which forms a 92-Å-long helix. The ARP-HSA interactions are reminiscent of contacts between actin and many binding partners and are quite different from those in the Arp2/3 complex. Rtt102 wraps around one side of the complex in a highly extended conformation that contacts both ARPs and therefore stabilizes the complex, yet functions to reduce by ∼2.4-fold the remodeling and ATPase activity of complexes containing the Snf2 ATPase domain. Thus, our structure provides a foundation for developing models of remodeler function, including mechanisms of coupling between ARPs and the ATPase translocation activity.

Indexed as

Chromatin Assembly and DisassemblyActinsAnimalsChromosomal Proteins, Non-HistoneCrystallography, X-RayDrosophila melanogasterMicrofilament ProteinsModels, MolecularMultiprotein ComplexesNucleosomesProtein BindingProtein MultimerizationProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsActinsChromosomal Proteins, Non-HistoneMicrofilament ProteinsMultiprotein ComplexesNucleosomesSaccharomyces cerevisiae ProteinsSWI-SNF-B chromatin-remodeling complexTranscription Factors

Identifiers

PMID23401505
PMCPMC3587198
OpenAlexW2103216631

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.