Evidence map›Paper›PMID 21673141›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Site-specific acetylation mark on an essential chromatin-remodeling complex promotes resistance to replication stress.

Georgette M Charles, Changbin Chen, Susan C Shih, Sean R Collins, Pedro Beltrao, Xin Zhang, Tanu Sharma, Song Tan, Alma L Burlingame, Nevan J Krogan and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Fungal-induced protein hyperacetylation in maize identified by acetylome profiling.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  5. Article
  6. Building a KATalogue of acetyllysine targeting and function.Briefings in functional genomics · 2016
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
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

12 authors at 2 institutions in 1 country.

Georgette M CharlesDepartment of Biochemistry and Biophysics, University of California, San Francisco, CA, 94158, USA.
Changbin Chen
Susan C Shih
Sean R Collins
Pedro Beltrao
Xin Zhang
Tanu Sharma
Song Tan
Alma L Burlingame
Nevan J Krogan
Hiten D Madhani
Geeta J Narlikar
University of California, San Francisco · USPennsylvania State University · US

Funding

STRUCTURE AND FUNCTION OF GENE REGULATORY COMPLEXESR01GM060489 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI TAN, SONG · 2000 to 2010
$2.4M
NIGMS NIH HHS R01 GM060489PHS HHS NCRR 001614
6 · The paper itself

Abstract

Recent work has identified several posttranslational modifications (PTMs) on chromatin-remodeling complexes. Compared with our understanding of histone PTMs, significantly less is known about the functions of PTMs on remodeling complexes, because identification of their specific roles often is hindered by the presence of redundant pathways. Remodels the Structure of Chromatin (RSC) is an essential, multifunctional ATP-dependent chromatin-remodeling enzyme of Saccharomyces cerevisiae that preferentially binds acetylated nucleosomes. RSC is itself acetylated by Gcn5 on lysine 25 (K25) of its Rsc4 subunit, adjacent to two tandem bromodomains. It has been shown that an intramolecular interaction between the acetylation mark and the proximal bromodomain inhibits binding of the second bromodomain to acetylated histone H3 tails. We report here that acetylation does not significantly alter the catalytic activity of RSC or its ability to recognize histone H3-acetylated nucleosomes preferentially in vitro. However, we find that Rsc4 acetylation is crucial for resistance to DNA damage in vivo. Epistatic miniarray profiling of the rsc4-K25R mutant reveals an interaction with mutants in the INO80 complex, a mediator of DNA damage and replication stress tolerance. In the absence of a core INO80 subunit, rsc4-K25R mutants display sensitivity to hydroxyurea and delayed S-phase progression under DNA damage. Thus, Rsc4 helps promote resistance to replication stress, and its single acetylation mark regulates this function. These studies offer an example of acetylation of a chromatin-remodeling enzyme controlling a biological output of the system rather than regulating its core enzymatic properties.

Indexed as

Chromatin Assembly and DisassemblyDNA ReplicationAcetylationDNA DamageLigandsSaccharomyces cerevisiaeS PhaseSubstrate SpecificityLigands

Identifiers

PMID21673141
PMCPMC3127919
OpenAlexW2122526183

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.