Overexpression of Rad51 protein stimulates homologous recombination and increases resistance of mammalian cells to ionizing radiation

Rad51 proteins share both structural and functional homologies with the bacterial recombinase RecA. The human Rad51 (HsRad51) is able to catalyse strand exchange between homologous DNA molecules in vitro. However the biological functions of Rad51 in mammals are largely unknown. In order to address t...

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Bibliographic Details
Published in:Nucleic acids research 1998-06, Vol.26 (12), p.2859-2864
Main Authors: Vispé, Stéphane, Cazaux, Christophe, Lesca, Claire, Defais, Martine
Format: Article
Language:English
Subjects:
Animals
CHO Cells
Cloning, Molecular
Cricetinae
DNA Damage
DNA Repair - physiology
DNA, Complementary - genetics
DNA-Binding Proteins - genetics
G2 Phase
Gamma Rays
Gene Expression
Molecular Sequence Data
Mutagens - pharmacology
Rad51 Recombinase
Radiation Tolerance - genetics
Recombination, Genetic - genetics
Sequence Analysis, DNA
Sequence Homology, Amino Acid
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Summary:Rad51 proteins share both structural and functional homologies with the bacterial recombinase RecA. The human Rad51 (HsRad51) is able to catalyse strand exchange between homologous DNA molecules in vitro. However the biological functions of Rad51 in mammals are largely unknown. In order to address this question, we have cloned hamster Rad51 cDNA and overexpressed the corresponding protein in CHO cells. We found that 2-3-fold overexpression of the protein stimulated the homologous recombination between integrated genes by 20-fold indicating that Rad51 is a functional and key enzyme of an intrachromosomal recombination pathway. Cells overexpressing Rad51 were resistant to ionizing radiation when irradiated in late S/G₂ phase of the cell cycle. This suggests that Rad51 participate in the repair of double-strand breaks most likely by homologous recombination involving sister chromatids formed after the S phase.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/26.12.2859