Evidence map›Paper›PMID 25787788›Full record

ArticleScientific reports2015

Mechanochemical regulations of RPA's binding to ssDNA.

Jin Chen, Shimin Le, Anindita Basu, Walter J Chazin, Jie Yan

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
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  9. Article
  10. Reduced Levels of Lagging Strand Polymerases Shape Stem Cell Chromatin.bioRxiv : the preprint server for biology · 2024
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  11. Replication of [AT/TA]Biochemistry · 2024
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  13. Replication of [AT/TA]bioRxiv : the preprint server for biology · 2023
    Article
  14. Article
  15. Article
  16. Article
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  18. 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 2 institutions in 2 countries.

Jin Chen1] Mechanobiology Institute, National University of Singapore, 117411 Singapore [2] Department of Physics, National University of Singapore, 117542 Singapore.
Shimin LeMechanobiology Institute, National University of Singapore, 117411 Singapore.
Anindita BasuDepartments of Biochemistry and Chemistry, Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.
Walter J ChazinDepartments of Biochemistry and Chemistry, Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.
Jie Yan1] Mechanobiology Institute, National University of Singapore, 117411 Singapore [2] Department of Physics, National University of Singapore, 117542 Singapore [3] Centre for Bioimaging Sciences, National University of Singapore, 117546 Singapore.
National University of Singapore · SGVanderbilt University · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
Structural Basis for RPA Functions in DNA ProcessingR01GM065484 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 2003 to 2015
$3.9M
NCI NIH HHS P01 CA092584NIGMS NIH HHS R01 GM065484NIGMS NIH HHS R01 GM65484NIGMS NIH HHS T32 GM008320
6 · The paper itself

Abstract

Replication protein A (RPA) is a ubiquitous eukaryotic single-stranded DNA (ssDNA) binding protein that serves to protect ssDNA from degradation and annealing, and as a template for recruitment of many downstream factors in virtually all DNA transactions in cell. During many of these transactions, DNA is tethered and is likely subject to force. Previous studies of RPA's binding behavior on ssDNA were conducted in the absence of force; therefore the RPA-ssDNA conformations regulated by force remain unclear. Here, using a combination of atomic force microscopy imaging and mechanical manipulation of single ssDNA tethers, we show that force mediates a switch of the RPA bound ssDNA from amorphous aggregation to a much more regular extended conformation. Further, we found an interesting non-monotonic dependence of the binding affinity on monovalent salt concentration in the presence of force. In addition, we discovered that zinc in micromolar concentrations drives ssDNA to a unique, highly stiff and more compact state. These results provide new mechanochemical insights into the influences and the mechanisms of action of RPA on large single ssDNA.

Indexed as

Biomechanical PhenomenaDNA ReplicationDNA, Single-StrandedKineticsModels, BiologicalProtein BindingReplication Protein ASodium ChlorideDNA, Single-StrandedReplication Protein ASodium Chloride

Identifiers

PMID25787788
PMCPMC4365408
OpenAlexW2026634019

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.