Evidence map›Paper›PMID 18310075›Full record

ArticleThe Journal of biological chemistry2008

Molecular anatomy of the recombination mediator function of Saccharomyces cerevisiae Rad52.

Changhyun Seong, Michael G Sehorn, Iben Plate, Idina Shi, Binwei Song, Peter Chi, Uffe Mortensen, Patrick Sung, Lumir Krejci

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

40 citing papers in PubMed, 57 citations in OpenAlex.

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  12. Unique molecular mechanisms for maintenance and alteration of genetic information in the budding yeastGenes and environment : the official journal of the Japanese Environmental Mutagen Society · 2017
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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

9 authors at 3 institutions in 3 countries.

Changhyun SeongDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
Michael G Sehorn
Iben Plate
Idina Shi
Binwei Song
Peter Chi
Uffe Mortensen
Patrick Sung
Lumir Krejci
Yale University · USTechnical University of Denmark · DKThe University of Texas Health Science Center at San Antonio · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
YEAST DNA REPAIR GENES AND PROTEINS OF THE RAD52 GROUPR01ES007061 · NIEHS · YALE UNIVERSITY · PI Patrick Sung · 1995 to 2026
$9.4M
FORMATION AND RESOLUTION OF RECOMBINATION INTERMEDIATESR01GM057814 · NIGMS · YALE UNIVERSITY · PI SUNG, PATRICK · 1999 to 2016
$4.2M
NCI NIH HHS P01 CA092584NCI NIH HHS P01CA92584NIEHS NIH HHS R01ES07061NIGMS NIH HHS R01GM57814Wellcome Trust GR076476
6 · The paper itself

Abstract

A helical filament of Rad51 on single-strand DNA (ssDNA), called the presynaptic filament, catalyzes DNA joint formation during homologous recombination. Rad52 facilitates presynaptic filament assembly, and this recombination mediator activity is thought to rely on the interactions of Rad52 with Rad51, the ssDNA-binding protein RPA, and ssDNA. The N-terminal region of Rad52, which has DNA binding activity and an oligomeric structure, is thought to be crucial for mediator activity and recombination. Unexpectedly, we find that the C-terminal region of Rad52 also harbors a DNA binding function. Importantly, the Rad52 C-terminal portion alone can promote Rad51 presynaptic filament assembly. The middle portion of Rad52 associates with DNA-bound RPA and contributes to the recombination mediator activity. Accordingly, expression of a protein species that harbors the middle and C-terminal regions of Rad52 in the rad52 Delta327 background enhances the association of Rad51 protein with a HO-made DNA double-strand break and partially complements the methylmethane sulfonate sensitivity of the mutant cells. Our results provide a mechanistic framework for rationalizing the multi-faceted role of Rad52 in recombination and DNA repair.

Indexed as

DNA Breaks, Double-StrandedDNA, FungalGenetic Complementation TestMicroscopy, ElectronMutant ProteinsProtein BindingProtein Structure, TertiaryRad51 RecombinaseRad52 DNA Repair and Recombination ProteinRecombination, GeneticReplication Protein ASaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA, FungalMutant ProteinsRad51 RecombinaseRad52 DNA Repair and Recombination ProteinRAD52 protein, S cerevisiaeReplication Protein ASaccharomyces cerevisiae Proteins

Identifiers

PMID18310075
PMCPMC2335352
OpenAlexW2006857908

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.