Abstract
The breast cancer susceptibility protein BRCA2 is essential for recombinational DNA repair. BRCA2 specifically binds to RAD51 via eight BRC repeat motifs and delivers RAD51 to double-stranded DNA breaks. In this study, a mammalian two-hybrid assay and competitive ELISA showed that the interaction between BRC repeat 4 (BRC4) and RAD51 was strengthened by the substitution of a single BRC4 amino acid from valine to isoleucine (V1532I). However, the cancer-associated V1532F mutant exhibited very weak interaction with RAD51. This study used a comparative analysis of BRC4 between animal species to identify V1532 as an important residue that interacts with RAD51.
Original language | English |
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Pages (from-to) | 1771-1777 |
Number of pages | 7 |
Journal | FEBS Letters |
Volume | 585 |
Issue number | 12 |
DOIs | |
Publication status | Published - Jun 23 2011 |
Keywords
- BRC repeat
- BRCA2
- Canine
- Homologous recombination
- RAD51
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology