Evidence map›Paper›PMID 24588663›Full record

ArticleBiochemistry2014

Dynamics of MutS-mismatched DNA complexes are predictive of their repair phenotypes.

Vanessa C DeRocco, Lauryn E Sass, Ruoyi Qiu, Keith R Weninger, Dorothy A Erie

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Mismatch Recognition byInternational journal of molecular sciences · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Studying protein-DNA interactions using atomic force microscopy.Seminars in cell & developmental biology · 2018
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Single-molecule motions and interactions in live cells reveal target search dynamics in mismatch repair.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. MutL traps MutS at a DNA mismatch.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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 1 institution in 1 country.

Vanessa C DeRoccoDepartment of Chemistry and ‡Curriculum in Applied Sciences and Engineering, The University of North Carolina at Chapel Hill , Chapel Hill, North Carolina 27599, United States.
Lauryn E Sass
Ruoyi Qiu
Keith R Weninger
Dorothy A Erie
North Carolina State University · US

Funding

Structure Function Studies of DNA Mismatch RepairR01GM079480 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ERIE, DOROTHY A · 2007 to 2017
$2.7M
Mechanistic studies of DNA repair and damage responseR01GM080294 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ERIE, DOROTHY A · 2009 to 2010
$565k
Single Molecule Studies of the Role of yMsh2-Msh6 in DNA Mismatch RepairF31GM087096 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DEROCCO, VANESSA CAROLYN · 2009 to 2011
$89k
NIGMS NIH HHS F31GM087096NIGMS NIH HHS GM079480NIGMS NIH HHS GM080294NIGMS NIH HHS R01 GM079480
6 · The paper itself

Abstract

MutS recognizes base-base mismatches and base insertions/deletions (IDLs) in newly replicated DNA. Specific interactions between MutS and these errors trigger a cascade of protein-protein interactions that ultimately lead to their repair. The inability to explain why different DNA errors are repaired with widely varying efficiencies in vivo remains an outstanding example of our limited knowledge of this process. Here, we present single-molecule Förster resonance energy transfer measurements of the DNA bending dynamics induced by Thermus aquaticus MutS and the E41A mutant of MutS, which is known to have error specific deficiencies in signaling repair. We compared three DNA mismatches/IDLs (T-bulge, GT, and CC) with repair efficiencies ranging from high to low. We identify three dominant DNA bending states [slightly bent/unbent (U), intermediately bent (I), and significantly bent (B)] and find that the kinetics of interconverting among states varies widely for different complexes. The increased stability of MutS-mismatch/IDL complexes is associated with stabilization of U and lowering of the B to U transition barrier. Destabilization of U is always accompanied by a destabilization of B, supporting the suggestion that B is a "required" precursor to U. Comparison of MutS and MutS-E41A dynamics on GT and the T-bulge suggests that hydrogen bonding to MutS facilitates the changes in base-base hydrogen bonding that are required to achieve the U state, which has been implicated in repair signaling. Taken together with repair propensities, our data suggest that the bending kinetics of MutS-mismatched DNA complexes may control the entry into functional pathways for downstream signaling of repair.

Indexed as

PhenotypeBacterial ProteinsDNA RepairFluorescence Resonance Energy TransferINDEL MutationMutS DNA Mismatch-Binding ProteinPredictive Value of TestsSignal TransductionThermusBacterial ProteinsMutS DNA Mismatch-Binding Protein

Identifiers

PMID24588663
PMCPMC3985873
OpenAlexW2329736351

What OpenQuestion holds

Textmetadata
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.