Evidence map›Paper›PMID 23097493›Full record

ArticleMolecular biology of the cell2012

Histone H1 compacts DNA under force and during chromatin assembly.

Botao Xiao, Benjamin S Freedman, Kelly E Miller, Rebecca Heald, John F Marko

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
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  4. Monitoring the compaction of single DNA molecules inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  6. Review
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  14. Epigenetics and autism spectrum disorder: A report of an autism case with mutation in H1 linker histone HIST1H1E and literature review.American journal of medical genetics. Part B, Neuropsychiatric genetics : the official publication of the International Society of Psychiatric Genetics · 2018
    Review
  15. Article
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  19. Forced unraveling of chromatin fibers with nonuniform linker DNA lengths.Journal of physics. Condensed matter : an Institute of Physics journal · 2015
    Article
  20. Article
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 2 institutions in 1 country.

Botao XiaoDepartment of Physics and Astronomy, Northwestern University, Evanston, IL 60208, USA. botao.xiao@childrens.harvard.edu
Benjamin S Freedman
Kelly E Miller
Rebecca Heald
John F Marko
University of California, Berkeley · USNorthwestern University · US

Funding

TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI WIDOM, JONATHAN · 2009 to 2013
$12.8M
STUDYING SPINDLE ASSEMBLY AND FUNCTION USING DNA BEADSR01GM057839 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HEALD, REBECCA W · 1998 to 2014
$3.3M
NCI NIH HHS U54 CA143869NCI NIH HHS U54CA143869-01NIGMS NIH HHS GM057839NIGMS NIH HHS R01 GM057839
6 · The paper itself

Abstract

Histone H1 binds to linker DNA between nucleosomes, but the dynamics and biological ramifications of this interaction remain poorly understood. We performed single-molecule experiments using magnetic tweezers to determine the effects of H1 on naked DNA in buffer or during chromatin assembly in Xenopus egg extracts. In buffer, nanomolar concentrations of H1 induce bending and looping of naked DNA at stretching forces below 0.6 pN, effects that can be reversed with 2.7-pN force or in 200 mM monovalent salt concentrations. Consecutive tens-of-nanometer bending events suggest that H1 binds to naked DNA in buffer at high stoichiometries. In egg extracts, single DNA molecules assemble into nucleosomes and undergo rapid compaction. Histone H1 at endogenous physiological concentrations increases the DNA compaction rate during chromatin assembly under 2-pN force and decreases it during disassembly under 5-pN force. In egg cytoplasm, histone H1 protects sperm nuclei undergoing genome-wide decondensation and chromatin assembly from becoming abnormally stretched or fragmented due to astral microtubule pulling forces. These results reveal functional ramifications of H1 binding to DNA at the single-molecule level and suggest an important physiological role for H1 in compacting DNA under force and during chromatin assembly.

Indexed as

Chromatin Assembly and DisassemblyAnimalsCell ExtractsCell NucleusDNAFemaleHistonesKineticsMaleNocodazoleNucleic Acid ConformationNucleosomesOvumPotassium ChlorideProtein BindingSpermatozoaCell ExtractsDNAHistonesNocodazoleNucleosomesPotassium ChlorideTubulin ModulatorsXenopus Proteins

Identifiers

PMID23097493
PMCPMC3521692
OpenAlexW2098816727

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.