Evidence map›Paper›PMID 28717009›Full record

ArticleThe Journal of biological chemistry2017

Acetylation on histone H3 lysine 9 mediates a switch from transcription initiation to elongation.

Leah A Gates, Jiejun Shi, Aarti D Rohira, Qin Feng, Bokai Zhu, Mark T Bedford, Cari A Sagum, Sung Yun Jung, Jun Qin, Ming-Jer Tsai and 4 more

Open access · hybridAbstract readValidation Study
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers.

0numbers the graph read from it
0cells of the map it votes in
154citing papers in PubMed
9.4field-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

154 citing papers in PubMed, 240 citations in OpenAlex.

  1. Review
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  5. Epigenetic regulation and ROS signaling in plant stress adaptation: an integrated framework.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026
    Review
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94 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

14 authors at 3 institutions in 1 country.

Leah A GatesFrom the Departments of Molecular and Cellular Biology and.
Jiejun ShiDivision of Biostatistics, Dan L. Duncan Cancer Center.
Aarti D RohiraFrom the Departments of Molecular and Cellular Biology and.
Qin FengFrom the Departments of Molecular and Cellular Biology and.
Bokai ZhuFrom the Departments of Molecular and Cellular Biology and.
Mark T Bedfordthe Department of Epigenetics and Molecular Carcinogenesis, University of Texas M.D. Anderson Cancer Center, Smithville, Texas 78957.
Cari A Sagumthe Department of Epigenetics and Molecular Carcinogenesis, University of Texas M.D. Anderson Cancer Center, Smithville, Texas 78957.
Sung Yun JungBiochemistry and Molecular Biology.
Jun QinFrom the Departments of Molecular and Cellular Biology and.
Ming-Jer TsaiFrom the Departments of Molecular and Cellular Biology and.
Sophia Y TsaiFrom the Departments of Molecular and Cellular Biology and.
Wei LiFrom the Departments of Molecular and Cellular Biology and.
Charles E FouldsFrom the Departments of Molecular and Cellular Biology and foulds@bcm.edu.
Bert W O'MalleyFrom the Departments of Molecular and Cellular Biology and berto@bcm.edu.
Dan L Duncan Comprehensive Cancer CenterThe University of Texas MD Anderson Cancer Center · USBaylor College of Medicine · US

Funding

Tumor BiologyP30CA125123 · NCI · BAYLOR COLLEGE OF MEDICINE · PI DAVID R ROWLEY · 2007 to 2026
$73.9M
REPRODUCTIVE HORMONES: BIOLOGICAL AND MOLECULAR ACTIONSR01HD008188 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI DAVID M LONARD, JOHN P LYDON · 1985 to 2026
$16.3M
REPRODUCTIVE BIOLOGY: REGULATORY MECHANISMST32HD007165 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI O'MALLEY, BERT W · 1985 to 2015
$5.6M
Computational and Experimental Modeling of Alternative PolyadenylationR01CA193466 · NCI · UNIVERSITY OF CALIFORNIA-IRVINE · PI LI, WEI · 2016 to 2025
$3.3M
Computational and Experimental Modeling of Epigenetic DNA MethylationR01HG007538 · NHGRI · UNIVERSITY OF CALIFORNIA-IRVINE · PI LI, WEI · 2014 to 2018
$1.9M
NCI NIH HHS P30 CA125123NCI NIH HHS R01 CA193466NHGRI NIH HHS R01 HG007538NICHD NIH HHS R01 HD008188NICHD NIH HHS T32 HD007165
6 · The paper itself

Abstract

The transition from transcription initiation to elongation is a key regulatory step in gene expression, which requires RNA polymerase II (pol II) to escape promoter proximal pausing on chromatin. Although elongation factors promote pause release leading to transcription elongation, the role of epigenetic modifications during this critical transition step is poorly understood. Two histone marks on histone H3, lysine 4 trimethylation (H3K4me3) and lysine 9 acetylation (H3K9ac), co-localize on active gene promoters and are associated with active transcription. H3K4me3 can promote transcription initiation, yet the functional role of H3K9ac is much less understood. We hypothesized that H3K9ac may function downstream of transcription initiation by recruiting proteins important for the next step of transcription. Here, we describe a functional role for H3K9ac in promoting pol II pause release by directly recruiting the super elongation complex (SEC) to chromatin. H3K9ac serves as a substrate for direct binding of the SEC, as does acetylation of histone H4 lysine 5 to a lesser extent. Furthermore, lysine 9 on histone H3 is necessary for maximal pol II pause release through SEC action, and loss of H3K9ac increases the pol II pausing index on a subset of genes in HeLa cells. At select gene promoters, H3K9ac loss or SEC depletion reduces gene expression and increases paused pol II occupancy. We therefore propose that an ordered histone code can promote progression through the transcription cycle, providing new mechanistic insight indicating that SEC recruitment to certain acetylated histones on a subset of genes stimulates the subsequent release of paused pol II needed for transcription elongation.

Indexed as

Chromatin Assembly and DisassemblyModels, BiologicalProtein Processing, Post-TranslationalTranscription Elongation, GeneticTranscription Initiation, GeneticAcetylationAmino Acid SubstitutionAnimalsDrosophilaDrosophila ProteinsEpigenesis, GeneticHeLa CellsHistonesHumansLysineMutationDrosophila ProteinsH3-3A protein, humanHistonesLysineNuclear ProteinsPeptide FragmentsRecombinant Fusion ProteinsRecombinant Proteinschromatingene expressionhistone acetylationRNA polymerase IIsuper elongation complextranscription

Identifiers

PMID28717009
PMCPMC5582839
OpenAlexW2735741666

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.