Evidence map›Paper›PMID 15014446›Full record

ArticleThe EMBO journal2004

Tandem bromodomains in the chromatin remodeler RSC recognize acetylated histone H3 Lys14.

Margaret Kasten, Heather Szerlong, Hediye Erdjument-Bromage, Paul Tempst, Michel Werner, Bradley R Cairns

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

117 citing papers in PubMed, 236 citations in OpenAlex.

  1. Article
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  4. DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024
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57 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

6 authors at 3 institutions in 2 countries.

Margaret KastenHoward Hughes Medical Institute and Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.
Heather Szerlong
Hediye Erdjument-Bromage
Paul Tempst
Michel Werner
Bradley R Cairns
University of Utah · USMemorial Sloan Kettering Cancer Center · USCentre de Génétique Moléculaire · FR

Funding

ANALYSIS OF THE CHROMATIN-REMODELING COMPLEX RSCR01GM060415 · NIGMS · UNIVERSITY OF UTAH · PI CAIRNS, BRADLEY R. · 1999 to 2011
$3.1M
NCI NIH HHS CA24014NIGMS NIH HHS GM60415NIGMS NIH HHS R01 GM060415
6 · The paper itself

Abstract

The coordination of chromatin remodeling with chromatin modification is a central topic in gene regulation. The yeast chromatin remodeling complex RSC bears multiple bromodomains, motifs for acetyl-lysine and histone tail interaction. Here, we identify and characterize Rsc4 and show that it bears tandem essential bromodomains. Conditional rsc4 bromodomain mutations were isolated, and were lethal in combination with gcn5Delta, whereas combinations with esa1 grew well. Replacements involving Lys14 of histone H3 (the main target of Gcn5), but not other H3 or H4 lysine residues, also conferred severe growth defects to rsc4 mutant strains. Importantly, wild-type Rsc4 bound an H3 tail peptide acetylated at Lys14, whereas a bromodomain mutant derivative did not. Loss of particular histone deacetylases suppressed rsc4 bromodomain mutations, suggesting that Rsc4 promotes gene activation. Furthermore, rsc4 mutants displayed defects in the activation of genes involved in nicotinic acid biosynthesis, cell wall integrity, and other pathways. Taken together, Rsc4 bears essential tandem bromodomains that rely on H3 Lys14 acetylation to assist RSC complex for gene activation.

Indexed as

Chromatin Assembly and DisassemblyAcetylationAmino Acid SequenceDNA-Binding ProteinsGene DeletionHistone AcetyltransferasesHistone DeacetylasesHistonesLysineMolecular Sequence DataMutagenesis, Site-Directedp300-CBP-Associated FactorProtein BindingProtein KinasesProtein Structure, TertiaryRepressor ProteinsDNA-Binding ProteinsGCN5 protein, S cerevisiaeHistone AcetyltransferasesHistone DeacetylasesHistonesLysinep300-CBP-Associated FactorProtein KinasesRepressor ProteinsRSC complex, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID15014446
PMCPMC381415
OpenAlexW1974426680

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.