Evidence map›Paper›PMID 25301943›Full record

ArticleThe Journal of biological chemistry2014

NuA4 links methylation of histone H3 lysines 4 and 36 to acetylation of histones H4 and H3.

Daniel S Ginsburg, Timi Elvuchio Anlembom, Jianing Wang, Sanket R Patel, Bing Li, Alan G Hinnebusch

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Set2 and H3K36 regulate thebioRxiv : the preprint server for biology · 2024
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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

6 authors at 1 institution in 1 country.

Daniel S GinsburgFrom the Biomedical Sciences Department, LIU Post, Brookville, New York 11548, daniel.ginsburg@liu.edu.
Timi Elvuchio AnlembomFrom the Biomedical Sciences Department, LIU Post, Brookville, New York 11548.
Jianing WangFrom the Biomedical Sciences Department, LIU Post, Brookville, New York 11548.
Sanket R PatelFrom the Biomedical Sciences Department, LIU Post, Brookville, New York 11548.
Bing Lithe Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, and.
Alan G Hinnebuschthe Laboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892.
National Institutes of Health · US

Funding

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
Mechanisms for chromatin modification during transcription elongationR01GM090077 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI LI, BING · 2010 to 2014
$1.5M
Intramural NIH HHSNIGMS NIH HHS R01 GM090077NIGMS NIH HHS R01GM090077
6 · The paper itself

Abstract

Cotranscriptional methylation of histone H3 lysines 4 and 36 by Set1 and Set2, respectively, stimulates interaction between nucleosomes and histone deacetylase complexes to block cryptic transcription in budding yeast. We previously showed that loss of all H3K4 and H3K36 methylation in a set1Δset2Δ mutant reduces interaction between native nucleosomes and the NuA4 lysine acetyltransferase (KAT) complex. We now provide evidence that NuA4 preferentially binds H3 tails mono- and dimethylated on H3K4 and di- and trimethylated on H3K36, an H3 methylation pattern distinct from that recognized by the RPD3C(S) and Hos2/Set3 histone deacetylase complexes (HDACs). Loss of H3K4 or H3K36 methylation in set1Δ or set2Δ mutants reduces NuA4 interaction with bulk nucleosomes in vitro and in vivo, and reduces NuA4 occupancy of transcribed coding sequences at particular genes. We also provide evidence that NuA4 acetylation of lysine residues in the histone H4 tail stimulates SAGA interaction with nucleosomes and its recruitment to coding sequences and attendant acetylation of histone H3 in vivo. Thus, H3 methylation exerts opposing effects of enhancing nucleosome acetylation by both NuA4 and SAGA as well as stimulating nucleosome deacetylation by multiple HDACs to maintain the proper level of histone acetylation in transcribed coding sequences.

Indexed as

AcetylationBlotting, WesternHistone AcetyltransferasesHistone DeacetylasesHistonesLysineMethylationMutationNucleosomesProtein BindingProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTrans-ActivatorsHistone AcetyltransferasesHistone DeacetylasesHistonesLysineNuA4 protein, S cerevisiaeNucleosomesProtein SubunitsSaccharomyces cerevisiae ProteinsSAGA complex, S cerevisiaeSet3 protein, S cerevisiaeTrans-ActivatorsAcetyltransferaseChromatin ModificationEsa1Histone AcetylaseHistone MethylationNuA4SAGASet1Set2Transcription Elongation Factor

Identifiers

PMID25301943
PMCPMC4239618
OpenAlexW2084064806

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.