Evidence map›Paper›PMID 22846989›Full record

ArticleThe Journal of biological chemistry2012

Reconstitution of the very short patch repair pathway from Escherichia coli.

Adam B Robertson, Steven W Matson

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. On the role of dcm and vsr in Escherichia coli adaptive mutation.Molecular genetics and genomics : MGG · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Isolating Escherichia coli strains for recombinant protein production.Cellular and molecular life sciences : CMLS · 2017
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Rate and molecular spectrum of spontaneous mutations in the bacterium Escherichia coli as determined by whole-genome sequencing.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

2 authors.

Adam B RobertsonDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.
Steven W Matson

Funding

ENZYMATIC MECHANISMS OF THE E. COLI HELICASESR01GM033476 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MATSON, STEVEN W · 1985 to 2010
$1.9M
NIGMS NIH HHS GM 33476NIGMS NIH HHS R01 GM033476
6 · The paper itself

Abstract

The Escherichia coli very short patch (VSP) repair pathway corrects thymidine-guanine mismatches that result from spontaneous hydrolytic deamination damage of 5-methyl cytosine. The VSP repair pathway requires the Vsr endonuclease, DNA polymerase I, a DNA ligase, MutS, and MutL to function at peak efficiency. The biochemical roles of most of these proteins in the VSP repair pathway have been studied extensively. However, these proteins have not been studied together in the context of VSP repair in an in vitro system. Using purified components of the VSP repair system in a reconstitution reaction, we have begun to develop an understanding of the role played by each of these proteins in the VSP repair pathway and have gained insights into their interactions. In this report we demonstrate an in vitro reconstitution of the VSP repair pathway using a plasmid DNA substrate. Surprisingly, the repair track length can be modulated by the concentration of DNA ligase. We propose roles for MutL and MutS in coordination of this repair pathway.

Indexed as

Adenosine TriphosphatasesDNA, BacterialDNA Ligase ATPDNA LigasesDNA Polymerase IDNA RepairEndodeoxyribonucleasesEscherichia coliEscherichia coli ProteinsMutL ProteinsMutS DNA Mismatch-Binding ProteinAdenosine TriphosphatasesDNA, BacterialDNA Ligase ATPDNA LigasesDNA Polymerase IEndodeoxyribonucleasesEscherichia coli ProteinsMutL protein, E coliMutL ProteinsMutS DNA Mismatch-Binding ProteinMutS protein, E colivsr endonuclease

Identifiers

PMID22846989
PMCPMC3463329

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.