Evidence map›Paper›PMID 25260587›Full record

ArticleNucleic acids research2014

RAD51B plays an essential role during somatic and meiotic recombination in Physcomitrella.

Florence Charlot, Liudmila Chelysheva, Yasuko Kamisugi, Nathalie Vrielynck, Anouchka Guyon, Aline Epert, Sylvia Le Guin, Didier G Schaefer, Andrew C Cuming, Mathilde Grelon and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

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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

11 authors at 5 institutions in 4 countries.

Florence CharlotINRA, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France AgroParisTech, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France.
Liudmila ChelyshevaINRA, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France AgroParisTech, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France.
Yasuko KamisugiCentre for Plant Sciences, Faculty of Biological Sciences, Leeds University, Leeds LS2 9JT, UK.
Nathalie VrielynckINRA, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France AgroParisTech, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France.
Anouchka GuyonINRA, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France AgroParisTech, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France.
Aline EpertINRA, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France AgroParisTech, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France.
Sylvia Le GuinINRA, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France AgroParisTech, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France.
Didier G SchaeferLaboratoire de Biologie Moleculaire et Cellulaire, Institut de Biologie, Universite de Neuchatel, rue Emile-Argand 11, CH-2007 Neuchatel, Switzerland.
Andrew C CumingCentre for Plant Sciences, Faculty of Biological Sciences, Leeds University, Leeds LS2 9JT, UK.
Mathilde GrelonINRA, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France AgroParisTech, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France.
Fabien NoguéINRA, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France AgroParisTech, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France fabien.nogue@versailles.inra.fr.
AgroParisTech · FRInstitut National de la Recherche Agronomique · MAInstitut Jean-Pierre Bourgin · FRUniversity of Leeds · GBUniversity of Neuchâtel · CH

Funding

Biotechnology and Biological Sciences Research Council BB/I006710/1
6 · The paper itself

Abstract

The eukaryotic RecA homologue Rad51 is a key factor in homologous recombination and recombinational repair. Rad51-like proteins have been identified in yeast (Rad55, Rad57 and Dmc1), plants and vertebrates (RAD51B, RAD51C, RAD51D, XRCC2, XRCC3 and DMC1). RAD51 and DMC1 are the strand-exchange proteins forming a nucleofilament for strand invasion, however, the function of the paralogues in the process of homologous recombination is less clear. In yeast the two Rad51 paralogues, Rad55 and Rad57, have been shown to be involved in somatic and meiotic HR and they are essential to the formation of the Rad51/DNA nucleofilament counterbalancing the anti-recombinase activity of the SRS2 helicase. Here, we examined the role of RAD51B in the model bryophyte Physcomitrella patens. Mutant analysis shows that RAD51B is essential for the maintenance of genome integrity, for resistance to DNA damaging agents and for gene targeting. Furthermore, we set up methods to investigate meiosis in Physcomitrella and we demonstrate that the RAD51B protein is essential for meiotic homologous recombination. Finally, we show that all these functions are independent of the SRS2 anti-recombinase protein, which is in striking contrast to what is found in budding yeast where the RAD51 paralogues are fully dependent on the SRS2 anti-recombinase function.

Indexed as

Homologous RecombinationBryopsidaDNA DamageDNA HelicasesGene DeletionMeiosisPhenotypePlant ProteinsRad51 RecombinaseDNA HelicasesPlant ProteinsRad51 Recombinase

Identifiers

PMID25260587
PMCPMC4231755
OpenAlexW2067883766

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.