Evidence map›Paper›PMID 21912525›Full record

ArticlePLoS genetics2011

Separation of recombination and SOS response in Escherichia coli RecA suggests LexA interaction sites.

Anbu K Adikesavan, Panagiotis Katsonis, David C Marciano, Rhonald Lua, Christophe Herman, Olivier Lichtarge

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

52 citing papers in PubMed, 85 citations in OpenAlex.

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  18. An Epistasis Analysis ofGenetics · 2020
    Article
  19. Two components of DNA replication-dependent LexA cleavage.The Journal of biological chemistry · 2020
    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

6 authors at 1 institution in 1 country.

Anbu K AdikesavanDepartment of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas, United States of America.
Panagiotis Katsonis
David C Marciano
Rhonald Lua
Christophe Herman
Olivier Lichtarge
Baylor College of Medicine · US

Funding

TRAINING PROGRAM IN COMPUTATIONAL BIOLOGY AND MEDICINET15LM007093 · NLM · RICE UNIVERSITY · PI Lydia E. Kavraki · 1992 to 2026
$20.8M
Functional Determinnats in G Protein-coupled ReceptorsR01GM066099 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI LICHTARGE, OLIVIER · 2003 to 2022
$7.5M
Comparative genomics of protein structure and functionR01GM079656 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI LICHTARGE, OLIVIER · 2007 to 2019
$4.3M
Training in Pharmacoinformatics(RMI)R90DK071505 · NIDDK · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI STANCEL, GEORGE M. · 2004 to 2008
$1.4M
NIDDK NIH HHS R90 DK071505NIGMS NIH HHS GM066099NIGMS NIH HHS GM079656NIGMS NIH HHS R01 GM066099NIGMS NIH HHS R01 GM079656NLM NIH HHS 5T15LM007093NLM NIH HHS T15 LM007093PHS HHS 5 R90 DKO71505
6 · The paper itself

Abstract

RecA plays a key role in homologous recombination, the induction of the DNA damage response through LexA cleavage and the activity of error-prone polymerase in Escherichia coli. RecA interacts with multiple partners to achieve this pleiotropic role, but the structural location and sequence determinants involved in these multiple interactions remain mostly unknown. Here, in a first application to prokaryotes, Evolutionary Trace (ET) analysis identifies clusters of evolutionarily important surface amino acids involved in RecA functions. Some of these clusters match the known ATP binding, DNA binding, and RecA-RecA homo-dimerization sites, but others are novel. Mutation analysis at these sites disrupted either recombination or LexA cleavage. This highlights distinct functional sites specific for recombination and DNA damage response induction. Finally, our analysis reveals a composite site for LexA binding and cleavage, which is formed only on the active RecA filament. These new sites can provide new drug targets to modulate one or more RecA functions, with the potential to address the problem of evolution of antibiotic resistance at its root.

Indexed as

Bacterial ProteinsEscherichia coliEvolution, MolecularHomologous RecombinationLexA Repressor ProteinMutagenesis, Site-DirectedProtein ConformationProtein Interaction Domains and MotifsRec A RecombinasesSerine EndopeptidasesSOS Response, GeneticsBacterial ProteinsLexA Repressor ProteinRec A RecombinasesSerine Endopeptidases

Identifiers

PMID21912525
PMCPMC3164682
OpenAlexW2100242429

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.