Evidence map›Paper›PMID 19506039›Full record

ArticleThe Journal of cell biology2009

Localization of recombination proteins and Srs2 reveals anti-recombinase function in vivo.

Rebecca C Burgess, Michael Lisby, Veronika Altmannova, Lumir Krejci, Patrick Sung, Rodney Rothstein

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
2.7field-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

64 citing papers in PubMed, 78 citations in OpenAlex.

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  6. Rad54 and Rdh54 prevent Srs2-mediated disruption of Rad51 presynaptic filaments.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  14. Meiosis-specific recombinase Dmc1 is a potent inhibitor of the Srs2 antirecombinase.Proceedings of the National Academy of Sciences of the United States of America · 2018
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4 more citing papers are in PubMed but not listed here.

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 4 institutions in 3 countries.

Rebecca C BurgessDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Michael Lisby
Veronika Altmannova
Lumir Krejci
Patrick Sung
Rodney Rothstein
Columbia University Irving Medical Center · USMasaryk University · CZUniversity of Copenhagen · DKYale University · US

Funding

YEAST DNA REPAIR GENES AND PROTEINS OF THE RAD52 GROUPR01ES007061 · NIEHS · YALE UNIVERSITY · PI Patrick Sung · 1995 to 2026
$9.4M
Mechanism of spontaneous and DSB-induced repairR37GM050237 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI ROTHSTEIN, RODNEY J. · 2005 to 2014
$6.0M
Genetics of the formation of repair &reombination fociR01GM067055 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI ROTHSTEIN, RODNEY J. · 2003 to 2014
$4.3M
MECHANISM OF SPONTANEOUS AND DSB-INDUCED REPAIRR01GM050237 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI ROTHSTEIN, RODNEY J. · 1993 to 2016
$3.0M
A Tripartite Approach to Elucidate Rdh54 functionF31GM073567 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI BURGESS, REBECCA C · 2004 to 2007
$131k
NIEHS NIH HHS ES07061NIEHS NIH HHS R01 ES007061NIGMS NIH HHS F31 GM073567NIGMS NIH HHS GM073567NIGMS NIH HHS GM50237NIGMS NIH HHS GM67055NIGMS NIH HHS R01 GM050237NIGMS NIH HHS R01 GM067055NIGMS NIH HHS R37 GM050237Wellcome TrustWellcome Trust GACR 203/09/H046Wellcome Trust GR07647
6 · The paper itself

Abstract

Homologous recombination (HR), although an important DNA repair mechanism, is dangerous to the cell if improperly regulated. The Srs2 "anti-recombinase" restricts HR by disassembling the Rad51 nucleoprotein filament, an intermediate preceding the exchange of homologous DNA strands. Here, we cytologically characterize Srs2 function in vivo and describe a novel mechanism for regulating the initiation of HR. We find that Srs2 is recruited separately to replication and repair centers and identify the genetic requirements for recruitment. In the absence of Srs2 activity, Rad51 foci accumulate, and surprisingly, can form in the absence of Rad52 mediation. However, these Rad51 foci do not represent repair-proficient filaments, as determined by recombination assays. Antagonistic roles for Rad52 and Srs2 in Rad51 filament formation are also observed in vitro. Furthermore, we provide evidence that Srs2 removes Rad51 indiscriminately from DNA, while the Rad52 protein coordinates appropriate filament reformation. This constant breakdown and rebuilding of filaments may act as a stringent quality control mechanism during HR.

Indexed as

Recombination, GeneticDNA Breaks, Double-StrandedDNA HelicasesDNA RepairDNA Repair EnzymesDNA ReplicationRad51 RecombinaseRad52 DNA Repair and Recombination ProteinRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesDNA HelicasesDNA Repair EnzymesRad51 RecombinaseRad52 DNA Repair and Recombination ProteinRAD54 protein, S cerevisiaeRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSRS2 protein, S cerevisiae

Identifiers

PMID19506039
PMCPMC2711611
OpenAlexW2119281566

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.