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

Charlot F, Chelysheva L, Kamisugi Y, Vrielynck N, Guyon A, Epert A, Le Guin S, Schaefer DG, Cuming AC, Grelon M, Nogué F - Nucleic Acids Res. (2014)

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: INRA, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France AgroParisTech, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France.

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The Physcomitrella genome encodes a RAD51B homologue. ClustalW alignment of the RAD51B proteins from Physcomitrella,Arabidopsis and human. The amino acid sequences of the proteins are shown in the single-letter code. Gaps are indicated by dashes. Conserved amino acids are black shaded and similar amino acids are grey shaded. The positions of the amino acids in each protein are shown at left. Black boxes indicate the positions of Walker motifs A and B. Accession numbers used in this analysis are as follows: PpRad51B (Phpat.025G051900.1.p), AtRad51B (NP_180423) and HsRad51B (AAC39723).
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Figure 2: The Physcomitrella genome encodes a RAD51B homologue. ClustalW alignment of the RAD51B proteins from Physcomitrella,Arabidopsis and human. The amino acid sequences of the proteins are shown in the single-letter code. Gaps are indicated by dashes. Conserved amino acids are black shaded and similar amino acids are grey shaded. The positions of the amino acids in each protein are shown at left. Black boxes indicate the positions of Walker motifs A and B. Accession numbers used in this analysis are as follows: PpRad51B (Phpat.025G051900.1.p), AtRad51B (NP_180423) and HsRad51B (AAC39723).

Mentions: Sequence homology searches of the Physcomitrella genome identified a single putative homologue for all the RAD51 paralogues except XRCC3 (Supplementary Figure S1). PpRAD51B is located on chromosome 25 (Phpat.025G051900) and our reverse transcriptase-PCR (RT-PCR) and Rapid Amplification of cDNA Ends (RACE) analyses of this gene, demonstrated that it consists of 12 exons and 11 introns (Figure 1A) and contains an open reading frame (ORF) of 362 amino acids (Figure 2). Phylogenetic analysis revealed that the protein encoded by PpRAD51B belongs effectively to the RAD51B family of proteins (Figure 2). The PpRAD51B protein has 46% and 36% sequence identity and 63% and 57% sequence similarity to AtRAD51B and HsRAD51B, respectively. There is extensive similarity among all the RAD51B polypeptides and PpRAD51B contained the characteristic features for RecA/Rad51 family proteins (Figure 2).


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

Charlot F, Chelysheva L, Kamisugi Y, Vrielynck N, Guyon A, Epert A, Le Guin S, Schaefer DG, Cuming AC, Grelon M, Nogué F - Nucleic Acids Res. (2014)

The Physcomitrella genome encodes a RAD51B homologue. ClustalW alignment of the RAD51B proteins from Physcomitrella,Arabidopsis and human. The amino acid sequences of the proteins are shown in the single-letter code. Gaps are indicated by dashes. Conserved amino acids are black shaded and similar amino acids are grey shaded. The positions of the amino acids in each protein are shown at left. Black boxes indicate the positions of Walker motifs A and B. Accession numbers used in this analysis are as follows: PpRad51B (Phpat.025G051900.1.p), AtRad51B (NP_180423) and HsRad51B (AAC39723).
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4231755&req=5

Figure 2: The Physcomitrella genome encodes a RAD51B homologue. ClustalW alignment of the RAD51B proteins from Physcomitrella,Arabidopsis and human. The amino acid sequences of the proteins are shown in the single-letter code. Gaps are indicated by dashes. Conserved amino acids are black shaded and similar amino acids are grey shaded. The positions of the amino acids in each protein are shown at left. Black boxes indicate the positions of Walker motifs A and B. Accession numbers used in this analysis are as follows: PpRad51B (Phpat.025G051900.1.p), AtRad51B (NP_180423) and HsRad51B (AAC39723).
Mentions: Sequence homology searches of the Physcomitrella genome identified a single putative homologue for all the RAD51 paralogues except XRCC3 (Supplementary Figure S1). PpRAD51B is located on chromosome 25 (Phpat.025G051900) and our reverse transcriptase-PCR (RT-PCR) and Rapid Amplification of cDNA Ends (RACE) analyses of this gene, demonstrated that it consists of 12 exons and 11 introns (Figure 1A) and contains an open reading frame (ORF) of 362 amino acids (Figure 2). Phylogenetic analysis revealed that the protein encoded by PpRAD51B belongs effectively to the RAD51B family of proteins (Figure 2). The PpRAD51B protein has 46% and 36% sequence identity and 63% and 57% sequence similarity to AtRAD51B and HsRAD51B, respectively. There is extensive similarity among all the RAD51B polypeptides and PpRAD51B contained the characteristic features for RecA/Rad51 family proteins (Figure 2).

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: INRA, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France AgroParisTech, Institut Jean-Pierre Bourgin UMR1318, Saclay Plant Sciences, Versailles, France.

Show MeSH
Related in: MedlinePlus