Evidence map›Paper›PMID 26750377›Full record

ArticleScientific reports2016

A quantitative investigation of linker histone interactions with nucleosomes and chromatin.

Alison E White, Aaron R Hieb, Karolin Luger

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
–field-weighted citation impact
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

48 citing papers in PubMed.

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  6. A DNA condensation code for linker histones.Proceedings of the National Academy of Sciences of the United States of America · 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

3 authors.

Alison E WhiteDepartment of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, CO 80303.
Aaron R HiebDepartment of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, CO 80303.
Karolin LugerDepartment of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, CO 80303.

Funding

project 3P01GM088409 · NIGMS · COLORADO STATE UNIVERSITY · PI NYBORG, JENNIFER K. · 2010 to 2014
$7.3M
Structure and Function of Nucleosome Assembly Protein 1R01GM067777 · NIGMS · UNIVERSITY OF COLORADO · PI LUGER, KAROLIN · 2003 to 2015
$3.7M
Howard Hughes Medical InstituteNIGMS NIH HHS GM067777NIGMS NIH HHS P01 GM088409NIGMS NIH HHS R01 GM067777
6 · The paper itself

Abstract

Linker histones such as H1 are abundant basic proteins that bind tightly to nucleosomes, thereby acting as key organizers of chromatin structure. The molecular details of linker histone interactions with the nucleosome, and in particular the contributions of linker DNA and of the basic C-terminal tail of H1, are controversial. Here we combine rigorous solution-state binding assays with native gel electrophoresis and Atomic Force Microscopy, to quantify the interaction of H1 with chromatin. We find that H1 binds nucleosomes and nucleosomal arrays with very tight affinity by recognizing a specific DNA geometry minimally consisting of a solitary nucleosome with a single ~18 base pair DNA linker arm. The association of H1 alters the conformation of trinucleosomes so that only one H1 can bind to the two available linker DNA regions. Neither incorporation of the histone variant H2A.Z, nor the presence of neighboring nucleosomes affects H1 affinity. Our data provide a comprehensive thermodynamic framework for this ubiquitous chromatin architectural protein.

Indexed as

AnimalsChromatinDNAHistonesMiceNucleosomesProtein BindingProtein Interaction Domains and MotifsChromatinDNAHistonesNucleosomes

Identifiers

PMID26750377
PMCPMC4707517

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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.