Evidence map›Paper›PMID 27010485›Full record

ArticleBiochemistry2016

Single-Molecule Studies of the Linker Histone H1 Binding to DNA and the Nucleosome.

Hongjun Yue, He Fang, Sijie Wei, Jeffrey J Hayes, Tae-Hee Lee

Abstract read
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

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  11. Physical Chemistry of Epigenetics: Single-Molecule Investigations.The journal of physical chemistry. B · 2019
    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

5 authors at 3 institutions in 1 country.

Hongjun YueDepartment of Chemistry, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.
He FangDepartment of Biochemistry and Biophysics, Rochester University Medical Center , Rochester, New York 14625, United States.
Sijie WeiDepartment of Chemistry, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.
Jeffrey J HayesDepartment of Biochemistry and Biophysics, Rochester University Medical Center , Rochester, New York 14625, United States.
Tae-Hee LeeDepartment of Chemistry, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.
Pennsylvania State University · USUniversity Medical Center · USUniversity of Rochester Medical Center · US

Funding

Histone Tall Interactions and Functions in ChromatinR01GM052426 · NIGMS · UNIVERSITY OF ROCHESTER · PI HAYES, JEFFREY J · 1995 to 2021
$6.2M
Dynamics of nucleosome assembly/disassembly affected by chromatin modificationsR01GM097286 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI LEE, TAE-HEE · 2011 to 2015
$1.4M
NIGMS NIH HHS GM052426NIGMS NIH HHS GM097286NIGMS NIH HHS R01 GM052426NIGMS NIH HHS R01 GM097286
6 · The paper itself

Abstract

Linker histone H1 regulates chromatin structure and gene expression. Investigating the dynamics and stoichiometry of binding of H1 to DNA and the nucleosome is crucial to elucidating its functions. Because of the abundant positive charges and the strong self-affinity of H1, quantitative in vitro studies of its binding to DNA and the nucleosome have generated results that vary widely and, therefore, should be interpreted in a system specific manner. We sought to overcome this limitation by developing a specially passivated microscope slide surface to monitor binding of H1 to DNA and the nucleosome at a single-molecule level. According to our measurements, the stoichiometry of binding of H1 to DNA and the nucleosome is very heterogeneous with a wide distribution whose averages are in reasonable agreement with previously published values. Our study also revealed that H1 does not dissociate from DNA or the nucleosome on a time scale of tens of minutes. We found that histone chaperone Nap1 readily dissociates H1 from DNA and superstoichiometrically bound H1 from the nucleosome, supporting a hypothesis whereby histone chaperones contribute to the regulation of the H1 profile in chromatin.

Indexed as

Models, MolecularAmino Acid SubstitutionAnimalsBinding, CompetitiveDNAHistonesImmobilized ProteinsKineticsLipid BilayersLiposomesMutationNucleic Acid ConformationNucleosome Assembly Protein 1NucleosomesPeptide FragmentsProtein ConformationDNAHistonesImmobilized ProteinsLipid BilayersLiposomesNAP1L1 protein, XenopusNucleosome Assembly Protein 1NucleosomesPeptide FragmentsRecombinant Fusion ProteinsRecombinant ProteinsXenopus Proteins

Identifiers

PMID27010485
PMCPMC5436050
OpenAlexW2305723624

What OpenQuestion holds

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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.