Evidence map›Paper›PMID 20439497›Full record

ArticleMolecular and cellular biology2010

Histone H2B C-terminal helix mediates trans-histone H3K4 methylation independent of H2B ubiquitination.

Mahesh B Chandrasekharan, Fu Huang, Yi-Chun Chen, Zu-Wen Sun

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 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 38 citations in OpenAlex.

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  9. Cancer prevention research (Philadelphia, Pa.) · 2020
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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

4 authors at 1 institution in 1 country.

Mahesh B ChandrasekharanDepartment of Biochemistry, Vanderbilt University School of Medicine, 613C Light Hall, Nashville, TN 37232, USA.
Fu Huang
Yi-Chun Chen
Zu-Wen Sun
Vanderbilt University · US

Funding

TISSUE CoreP50CA098131 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI PARK, BEN HO, PIETENPOL, JENNIFER A · 2003 to 2024
$48.7M
Functions of Histone Ubiquitination and MethylationR01CA109355 · NCI · VANDERBILT UNIVERSITY · PI SUN, ZU-WEN · 2006 to 2010
$1.2M
NCI NIH HHS 5P0CA098131NCI NIH HHS P50 CA098131NCI NIH HHS R01 CA109355NCI NIH HHS R01CA109355
6 · The paper itself

Abstract

The trans-histone regulatory cross talk between H2BK123 ubiquitination (H2Bub1) and H3K4 and H3K79 methylation is not fully understood. In this study, we report that the residues arginine 119 and threonine 122 in the H2B C-terminal helix are important for transcription and cell growth and play a direct role in controlling H2Bub1 and H3K4 methylation. These residues modulate H2Bub1 levels by controlling the chromatin binding and activities of the deubiquitinases. Furthermore, we find an uncoupling of the H2Bub1-mediated coregulation of both H3K4 and -K79 methylation, as these H2B C-terminal helix residues are part of a distinct surface that affects only Set1-COMPASS (complex proteins associated with Set1)-mediated H3K4 methylation without affecting the functions of Dot1. Importantly, we also find that these residues interact with Spp1 and control the chromatin association, integrity, and overall stability of Set1-COMPASS independent of H2Bub1. Therefore, we have uncovered a novel role for the H2B C-terminal helix in the trans-histone cross talk as a binding surface for Set1-COMPASS. We provide further insight into the trans-histone cross talk and propose that H2Bub1 stabilizes the nucleosome by preventing H2A-H2B eviction and, thereby, retains the "docking site" for Set1-COMPASS on chromatin to maintain its stable chromatin association, complex stability, and processive methylation.

Indexed as

Amino Acid SequenceChromatinDNA-Binding ProteinsGene Expression Regulation, FungalGene SilencingHistone-Lysine N-MethyltransferaseHistonesLysineMethylationModels, MolecularMolecular Sequence DataMutationProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTelomereChromatinDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistonesLysineSaccharomyces cerevisiae ProteinsSET1 protein, S cerevisiaeSPP1 protein, S cerevisiae

Identifiers

PMID20439497
PMCPMC2897581
OpenAlexW2097698426

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.