Evidence map›Paper›PMID 21427084›Full record

ArticleNucleic acids research2011

Force-driven unbinding of proteins HU and Fis from DNA quantified using a thermodynamic Maxwell relation.

Botao Xiao, Houyin Zhang, Reid C Johnson, John F Marko

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
5.3field-weighted citation impact, top 5% 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

27 citing papers in PubMed, 44 citations in OpenAlex.

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  8. DNA Supercoiling: an Ancestral Regulator of Gene Expression in Pathogenic Bacteria?Computational and structural biotechnology journal · 2019
    Review
  9. Review
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  16. ParB spreading requires DNA bridging.Genes & development · 2014
    Article
  17. Article
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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 3 institutions in 2 countries.

Botao XiaoDepartment of Physics and Astronomy, Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA. botaoshaw@hotmail.com
Houyin Zhang
Reid C Johnson
John F Marko
University of California, Los Angeles · USAstronomy and Space · AUNorthwestern University · US

Funding

TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI MARKO, JOHN F · 2009 to 2013
$12.8M
Molecular Analysis of Site Specific DNA RecombinationR37GM038509 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI JOHNSON, REID C · 2005 to 2014
$6.6M
MOLECULAR ANALYSIS OF SITE-SPECIFIC DNA RECOMBINATIONR01GM038509 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI JOHNSON, REID C · 1987 to 2018
$4.7M
NCI NIH HHS U54CA143869-01NIGMS NIH HHS GM038509NIGMS NIH HHS R37 GM038509
6 · The paper itself

Abstract

Determining numbers of proteins bound to large DNAs is important for understanding their chromosomal functions. Protein numbers may be affected by physical factors such as mechanical forces generated in DNA, e.g. by transcription or replication. We performed single-DNA stretching experiments with bacterial nucleoid proteins HU and Fis, verifying that the force-extension measurements were in thermodynamic equilibrium. We, therefore, could use a thermodynamic Maxwell relation to deduce the change of protein number on a single DNA due to varied force. For the binding of both HU and Fis under conditions studied, numbers of bound proteins decreased as force was increased. Our experiments showed that most of the bound HU proteins were driven off the DNA at 6.3 pN for HU concentrations lower than 150 nM; our HU data were fit well by a statistical-mechanical model of protein-induced bending of DNA. In contrast, a significant amount of Fis proteins could not be forced off the DNA at forces up to 12 pN and Fis concentrations up to 20 nM. This thermodynamic approach may be applied to measure changes in numbers of a wide variety of molecules bound to DNA or other polymers. Force-dependent DNA binding by proteins suggests mechano-chemical mechanisms for gene regulation.

Indexed as

ThermodynamicsDNADNA-Binding ProteinsEscherichia coli ProteinsFactor For Inversion Stimulation ProteinModels, StatisticalProtein BindingDNADNA-Binding ProteinsEscherichia coli ProteinsFactor For Inversion Stimulation ProteinFis protein, E colihns protein, E coli

Identifiers

PMID21427084
PMCPMC3141252
OpenAlexW2065020575

What OpenQuestion holds

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LicenceCC BY-NC
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.