Evidence map›Paper›PMID 26648124›Full record

ArticleNature communications2015

Linker histone H1 and H3K56 acetylation are antagonistic regulators of nucleosome dynamics.

Morgan Bernier, Yi Luo, Kingsley C Nwokelo, Michelle Goodwin, Sarah J Dreher, Pei Zhang, Mark R Parthun, Yvonne Fondufe-Mittendorf, Jennifer J Ottesen, Michael G Poirier

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed, 60 citations in OpenAlex.

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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

10 authors at 2 institutions in 1 country.

Morgan BernierDepartment of Physics, The Ohio State University, Columbus, Ohio 43210, USA.
Yi LuoBiophysics Graduate Program, The Ohio State University, Columbus, Ohio 43210, USA.
Kingsley C NwokeloDepartment of Physics, The Ohio State University, Columbus, Ohio 43210, USA.
Michelle GoodwinDepartment of Physics, The Ohio State University, Columbus, Ohio 43210, USA.
Sarah J DreherThe Ohio State Biochemistry Program, The Ohio State University, Columbus, Ohio 43210, USA.
Pei ZhangDepartment of Biological Chemistry and Pharmacology, The Ohio State University, Columbus, Ohio 43210, USA.
Mark R ParthunDepartment of Biological Chemistry and Pharmacology, The Ohio State University, Columbus, Ohio 43210, USA.
Yvonne Fondufe-MittendorfDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky 40536, USA.
Jennifer J OttesenBiophysics Graduate Program, The Ohio State University, Columbus, Ohio 43210, USA.
Michael G PoirierDepartment of Physics, The Ohio State University, Columbus, Ohio 43210, USA.
The Ohio State University · USUniversity of Kentucky · US

Funding

Type B Histone Acetyltransferases and the Assembly of Chromatin StructureR01GM062970 · NIGMS · OHIO STATE UNIVERSITY · PI PARTHUN, MARK R · 2001 to 2018
$5.1M
Mechanisms of Chromatin Transcriptional RegulationR01GM083055 · NIGMS · OHIO STATE UNIVERSITY · PI POIRIER, MICHAEL GUY · 2008 to 2016
$2.7M
The role of chromatin structural and epigenetic changes in arsenic-induced gene expressionR01ES024478 · NIEHS · UNIVERSITY OF KENTUCKY · PI FONDUFE-MITTENDORF, YVONNE NSOKIKA · 2015 to 2019
$1.8M
NIEHS NIH HHS R01 ES024478NIGMS NIH HHS R01 GM062970NIGMS NIH HHS R01 GM083055NIGMS NIH HHS R01 GM62970
6 · The paper itself

Abstract

H1 linker histones are highly abundant proteins that compact nucleosomes and chromatin to regulate DNA accessibility and transcription. However, the mechanisms that target H1 regulation to specific regions of eukaryotic genomes are unknown. Here we report fluorescence measurements of human H1 regulation of nucleosome dynamics and transcription factor (TF) binding within nucleosomes. H1 does not block TF binding, instead it suppresses nucleosome unwrapping to reduce DNA accessibility within H1-bound nucleosomes. We then investigated H1 regulation by H3K56 and H3K122 acetylation, two transcriptional activating histone post translational modifications (PTMs). Only H3K56 acetylation, which increases nucleosome unwrapping, abolishes H1.0 reduction of TF binding. These findings show that nucleosomes remain dynamic, while H1 is bound and H1 dissociation is not required for TF binding within the nucleosome. Furthermore, our H3K56 acetylation measurements suggest that a single-histone PTM can define regions of the genome that are not regulated by H1.

Indexed as

AcetylationAmino Acid MotifsChromatinHistonesHumansNucleosomesTranscription FactorsChromatinHistonesNucleosomesTranscription Factors

Identifiers

PMID26648124
PMCPMC4682114
OpenAlexW2336701517

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.