Evidence map›Paper›PMID 21097894›Full record

ArticleNucleic acids research2011

Concentration-dependent exchange accelerates turnover of proteins bound to double-stranded DNA.

John S Graham, 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 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

108 citing papers in PubMed, 159 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. TDP-43 controls RNA structure through high affinity lattice interactions.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. The mechanism of mRNA activation.bioRxiv : the preprint server for biology · 2023
    Article
  12. Article
  13. IHF and Fis asInternational journal of molecular sciences · 2023
    Review
  14. Multiple RNA- and DNA-binding proteins exhibit direct transfer of polynucleotides with implications for target-site search.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. PRC2 direct transfer from G-quadruplex RNA to dsDNA has implications for RNA-binding chromatin modifiers.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

48 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 1 country.

John S GrahamDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500, USA. john-graham@northwestern.edu
Reid C Johnson
John F Marko
University of California, Los Angeles · USNorthwestern 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

The multistep kinetics through which DNA-binding proteins bind their targets are heavily studied, but relatively little attention has been paid to proteins leaving the double helix. Using single-DNA stretching and fluorescence detection, we find that sequence-neutral DNA-binding proteins Fis, HU and NHP6A readily exchange with themselves and with each other. In experiments focused on the Escherichia coli nucleoid-associated protein Fis, only a small fraction of protein bound to DNA spontaneously dissociates into protein-free solution. However, if Fis is present in solution, we find that a concentration-dependent exchange reaction occurs which turns over the bound protein, with a rate of k(exch) = 6 × 10(4) M(-1)s(-1). The bacterial DNA-binding protein HU and the yeast HMGB protein NHP6A display the same phenomenon of protein in solution accelerating dissociation of previously bound labeled proteins as exchange occurs. Thus, solvated proteins can play a key role in facilitating removal and renewal of proteins bound to the double helix, an effect that likely plays a major role in promoting the turnover of proteins bound to DNA in vivo and, therefore, in controlling the dynamics of gene regulation.

Indexed as

DNADNA-Binding ProteinsEscherichia coli ProteinsFactor For Inversion Stimulation ProteinHMGN ProteinsKineticsMicroscopy, FluorescenceProtein BindingSaccharomyces cerevisiae ProteinsDNADNA-Binding ProteinsEscherichia coli ProteinsFactor For Inversion Stimulation ProteinFis protein, E coliHMGN Proteinshns protein, E coliNHP6A protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID21097894
PMCPMC3064784
OpenAlexW2070181970

What OpenQuestion holds

Textmetadata
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.