Evidence map›Paper›PMID 22921573›Full record

ArticleDNA repair2012

Unwinding of synthetic replication and recombination substrates by Srs2.

Victoria Marini, Lumir Krejci

Abstract read
In one paragraph

Article in DNA repair, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

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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

2 authors.

Victoria MariniDepartment of Biology, Masaryk University, Kamenice, Brno, Czech Republic.
Lumir Krejci

Funding

Wellcome Trust
6 · The paper itself

Abstract

The budding yeast Srs2 protein possesses 3' to 5' DNA helicase activity and channels untimely recombination to post-replication repair by removing Rad51 from ssDNA. However, it also promotes recombination via a synthesis-dependent strand-annealing pathway (SDSA). Furthermore, at the replication fork, Srs2 is required for fork progression and prevents the instability of trinucleotide repeats. To better understand the multiple roles of the Srs2 helicase during these processes, we analysed the ability of Srs2 to bind and unwind various DNA substrates that mimic structures present during DNA replication and recombination. While leading or lagging strands were efficiently unwound, the presence of ssDNA binding protein RPA presented an obstacle for Srs2 translocation. We also tested the preferred directionality of unwinding of various substrates and studied the effect of Rad51 and Mre11 proteins on Srs2 helicase activity. These biochemical results help us understand the possible role of Srs2 in the processing of stalled or blocked replication forks as a part of post-replication repair as well as homologous recombination (HR).

Indexed as

DNA ReplicationHomologous RecombinationDNA, CruciformDNA HelicasesDNA, Single-StrandedEndodeoxyribonucleasesExodeoxyribonucleasesGene DeletionRad51 RecombinaseReplication Protein ASaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA, CruciformDNA HelicasesDNA, Single-StrandedEndodeoxyribonucleasesExodeoxyribonucleasesMRE11 protein, S cerevisiaeRAD51 protein, S cerevisiaeRad51 RecombinaseReplication Protein ARFA1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSRS2 protein, S cerevisiae

Identifiers

PMID22921573
PMCPMC3484393

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.