Evidence map›Paper›PMID 20498280›Full record

ArticleMolecular and cellular biology2010

Novel trans-tail regulation of H2B ubiquitylation and H3K4 methylation by the N terminus of histone H2A.

Suting Zheng, John J Wyrick, Joseph C Reese

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 47 citations in OpenAlex.

  1. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  2. DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024
    Review
  3. Review
  4. Review
  5. Histone Tail Conformations: A Fuzzy Affair with DNA.Trends in biochemical sciences · 2021
    Review
  6. Insights on the regulation of the MLL/SET1 family histone methyltransferases.Biochimica et biophysica acta. Gene regulatory mechanisms · 2020
    Review
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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

3 authors at 2 institutions in 1 country.

Suting ZhengDepartment of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, Penn State University, University Park, Pennsylvania 16802, USA.
John J Wyrick
Joseph C Reese
Pennsylvania State University · USWashington State University · US

Funding

REGULATION OF DNA DAMAGE INDUCED GENES BY YEAST TAFIISR01GM058672 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI REESE, JOSEPH C · 1999 to 2019
$6.5M
NIGMS NIH HHS GM58672NIGMS NIH HHS R01 GM058672
6 · The paper itself

Abstract

Chromatin is regulated by cross talk among different histone modifications, which can occur between residues within the same tail or different tails in the nucleosome. The latter is referred to as trans-tail regulation, and the best-characterized example of this is the dependence of H3 methylation on H2B ubiquitylation. Here we describe a novel form of trans-tail regulation of histone modifications involving the N-terminal tail of histone H2A. Mutating or deleting residues in the N-terminal tail of H2A reduces H2B ubiquitylation and H3K4 methylation but does not affect the recruitment of the modifying enzymes, Rad6/Bre1 and COMPASS, to genes. The H2A tail is required for the incorporation of Cps35 into COMPASS, and increasing the level of ubiquitylated H2B in H2A tail mutants suppresses the H3K4 methylation defect, suggesting that the H2A tail regulates H2B-H3 cross talk. We mapped the region primarily responsible for this regulation to the H2A repression domain, HAR. The HAR and K123 of H2B are in close proximity to each other on the nucleosome, suggesting that they form a docking site for the ubiquitylation machinery. Interestingly, the HAR is partially occluded by nucleosomal DNA, suggesting that the function of the H2A cross talk pathway is to restrict histone modifications to nucleosomes altered by transcription.

Indexed as

Gene Expression ProfilingGenes, FungalHistone-Lysine N-MethyltransferaseHistonesMethylationModels, BiologicalModels, MolecularMutationNucleosomesProtein Interaction Domains and MotifsProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionUbiquitinationUbiquitin-Conjugating EnzymesBre1 protein, S cerevisiaeHistone-Lysine N-MethyltransferaseHistonesNucleosomesRAD6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSWD2 protein, S cerevisiaeUbiquitin-Conjugating Enzymes

Identifiers

PMID20498280
PMCPMC2897545
OpenAlexW2158835357

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.