Evidence map›Paper›PMID 22177115›Full record

ArticleCurrent biology : CB2012

The Rpd3 core complex is a chromatin stabilization module.

Xiao-Fen Chen, Benjamin Kuryan, Tasuku Kitada, Nancy Tran, Jing-Yu Li, Siavash Kurdistani, Michael Grunstein, Bing Li, Michael Carey

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

39 citing papers in PubMed, 52 citations in OpenAlex.

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  10. Class I histone deacetylase complex: Structure and functional correlates.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

9 authors at 2 institutions in 1 country.

Xiao-Fen ChenDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095-1737, USA.
Benjamin Kuryan
Tasuku Kitada
Nancy Tran
Jing-Yu Li
Siavash Kurdistani
Michael Grunstein
Bing Li
Michael Carey
University of California, Los Angeles · USThe University of Texas Southwestern Medical Center · US

Funding

Mechanisms for chromatin modification during transcription elongationR01GM090077 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI LI, BING · 2010 to 2014
$1.5M
Elongation of Yeast Pol II Through NucleosomesR01GM085002 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CAREY, MICHAEL F · 2008 to 2011
$1.2M
NIGMS NIH HHS 1R01GM085002NIGMS NIH HHS R01 GM085002NIGMS NIH HHS R01 GM090077NIGMS NIH HHS R01GM090077
6 · The paper itself

Abstract

The S. cerevisiae Rpd3 large (Rpd3L) and small (Rpd3S) histone deacetylase (HDAC) complexes are prototypes for understanding transcriptional repression in eukaryotes [1]. The current view is that they function by deacetylating chromatin, thereby limiting accessibility of transcriptional factors to the underlying DNA. However, an Rpd3 catalytic mutant retains substantial repression capability when targeted to a promoter as a LexA fusion protein [2]. We investigated the HDAC-independent properties of the Rpd3 complexes biochemically and discovered a chaperone function, which promotes histone deposition onto DNA, and a novel activity, which prevents nucleosome eviction but not remodeling mediated by the ATP-dependent RSC complex. These HDAC-independent activities inhibit Pol II transcription on a nucleosomal template. The functions of the endogenous Rpd3 complexes can be recapitulated with recombinant Rpd3 core complex comprising Sin3, Rpd3, and Ume1. To test the hypothesis that Rpd3 contributes to chromatin stabilization in vivo, we measured histone H3 density genomewide and found that it was reduced at promoters in an Rpd3 deletion mutant but partially restored in a catalytic mutant. Importantly, the effects on H3 density are most apparent on RSC-enriched genes [3]. Our data suggest that the Rpd3 core complex could contribute to repression via a novel nucleosome stabilization function.

Indexed as

Adenosine TriphosphateChromatinDNA-Binding ProteinsGene Expression Regulation, FungalGenome, FungalHistone DeacetylasesHistonesMolecular ChaperonesNucleosomesRepressor ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsAdenosine TriphosphateChromatinDNA-Binding ProteinsHistone DeacetylasesHistonesMolecular ChaperonesNucleosomesRepressor ProteinsRPD3 protein, S cerevisiaeRSC complex, S cerevisiaeSaccharomyces cerevisiae ProteinsSIN3 protein, S cerevisiaeTranscription FactorsUME1 protein, S cerevisiae

Identifiers

PMID22177115
PMCPMC3758238
OpenAlexW2085885847

What OpenQuestion holds

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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.