Evidence map›Paper›PMID 20670892›Full record

ArticleMolecular cell2010

Phosphorylated Pol II CTD recruits multiple HDACs, including Rpd3C(S), for methylation-dependent deacetylation of ORF nucleosomes.

Chhabi K Govind, Hongfang Qiu, Daniel S Ginsburg, Chun Ruan, Kimberly Hofmeyer, Cuihua Hu, Venkatesh Swaminathan, Jerry L Workman, Bing Li, Alan G Hinnebusch

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 156 papers.

0numbers the graph read from it
0cells of the map it votes in
156citing papers in PubMed
10.5field-weighted citation impact, top 1% 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

156 citing papers in PubMed, 227 citations in OpenAlex.

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  10. Structure of histone deacetylase complex Rpd3S bound to nucleosome.Nature structural & molecular biology · 2023
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96 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

10 authors at 3 institutions in 1 country.

Chhabi K GovindLaboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, MD 20892, USA. govind@oakland.edu
Hongfang Qiu
Daniel S Ginsburg
Chun Ruan
Kimberly Hofmeyer
Cuihua Hu
Venkatesh Swaminathan
Jerry L Workman
Bing Li
Alan G Hinnebusch
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USStowers Institute for Medical Research · USThe University of Texas Southwestern Medical Center · US

Funding

Translational & Transcriptional Control Of Gene Expression By Nutrients In YeastZIAHD001004 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI HINNEBUSCH, ALAN G · 2009 to 2025
$34.4M
Transcriptional Regulation of Gene ExpressionZIAHD008899 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI HINNEBUSCH, ALAN G · 2010 to 2025
$11.6M
Intramural NIH HHS ZIA HD001004
6 · The paper itself

Abstract

Methylation of histone H3 by Set1 and Set2 is required for deacetylation of nucleosomes in coding regions by histone deacetylase complexes (HDACs) Set3C and Rpd3C(S), respectively. We report that Set3C and Rpd3C(S) are cotranscriptionally recruited in the absence of Set1 and Set2, but in a manner stimulated by Pol II CTD kinase Cdk7/Kin28. Consistently, Rpd3C(S) and Set3C interact with Ser5-phosphorylated Pol II and histones in extracts, but only the histone interactions require H3 methylation. Moreover, reconstituted Rpd3C(S) binds specifically to Ser5-phosphorylated CTD peptides in vitro. Hence, whereas interaction with methylated H3 residues is required for Rpd3C(S) and Set3C deacetylation activities, their cotranscriptional recruitment is stimulated by the phosphorylated CTD. We further demonstrate that Rpd3, Hos2, and Hda1 have overlapping functions in deacetylating histones and suppressing cotranscriptional histone eviction. A strong correlation between increased acetylation and lower histone occupancy in HDA mutants implies that histone acetylation is important for nucleosome eviction.

Indexed as

Cyclin-Dependent KinasesHistone DeacetylasesHistone-Lysine N-MethyltransferaseHistonesMethylationMethyltransferasesNucleosomesOpen Reading FramesPhosphorylationRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCyclin-Dependent KinasesHDA1 protein, S cerevisiaeHistone DeacetylasesHistone-Lysine N-MethyltransferaseHistonesHOS2 protein, S cerevisiaeKin28 protein kinase, S cerevisiaeMethyltransferasesNucleosomesRNA Polymerase IIRPD3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSET1 protein, S cerevisiaeSet2 protein, S cerevisiaeSet3 protein, S cerevisiae

Identifiers

PMID20670892
PMCPMC2937259
OpenAlexW1963532124

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.