Evidence map›Paper›PMID 22241777›Full record

ArticleNucleic acids research2012

Stoichiometry of MutS and MutL at unrepaired mismatches in vivo suggests a mechanism of repair.

Marina Elez, Miroslav Radman, Ivan Matic

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

34 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. MutS sliding clamps on an uncertain track to DNA mismatch repair.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. G3 (Bethesda, Md.) · 2020
    Article
  12. Recurrent mismatch binding by MutS mobile clamps on DNA localizes repair complexes nearby.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Dynamic human MutSα-MutLα complexes compact mismatched DNA.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Real-time dynamics of mutagenesis reveal the chronology of DNA repair and damage tolerance responses in single cells.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Single-cell mutagenic responses and cell death revealed in real time.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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

3 authors at 2 institutions in 2 countries.

Marina ElezUniversité Paris-Descartes, Sorbonne Paris Cité, Inserm Unit 1001, 75015 Paris, France. marina.elez@inserm.fr
Miroslav Radman
Ivan Matic
Mediterranean Institute for Life Sciences · HRDélégation Paris 5 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mismatch repair (MMR) is an evolutionarily conserved DNA repair system, which corrects mismatched bases arising during DNA replication. MutS recognizes and binds base pair mismatches, while the MutL protein interacts with MutS-mismatch complex and triggers MutH endonuclease activity at a distal-strand discrimination site on the DNA. The mechanism of communication between these two distal sites on the DNA is not known. We used functional fluorescent MMR proteins, MutS and MutL, in order to investigate the formation of the fluorescent MMR protein complexes on mismatches in real-time in growing Escherichia coli cells. We found that MutS and MutL proteins co-localize on unrepaired mismatches to form fluorescent foci. MutL foci were, on average, 2.7 times more intense than the MutS foci co-localized on individual mismatches. A steric block on the DNA provided by the MutHE56A mutant protein, which binds to but does not cut the DNA at the strand discrimination site, decreased MutL foci fluorescence 3-fold. This indicates that MutL accumulates from the mismatch site toward strand discrimination site along the DNA. Our results corroborate the hypothesis postulating that MutL accumulation assures the coordination of the MMR activities between the mismatch and the strand discrimination site.

Indexed as

Base Pair MismatchDNA Mismatch RepairAdenosine TriphosphatasesDNAEscherichia coliEscherichia coli ProteinsFluorescent DyesLuminescent ProteinsMutL ProteinsMutS DNA Mismatch-Binding ProteinRecombinant Fusion ProteinsAdenosine TriphosphatasesDNAEscherichia coli ProteinsFluorescent DyesLuminescent ProteinsMutL protein, E coliMutL ProteinsMutS DNA Mismatch-Binding ProteinMutS protein, E coliRecombinant Fusion Proteins

Identifiers

PMID22241777
PMCPMC3351158
OpenAlexW2117000131

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.