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Multiple possible sites of BRAC2 interacting with DNA repair protein RAD51
Author(s) -
Katagiri Toyomasa,
Saito Hiroko,
Shinohara Akira,
Ogawa Hideyuki,
Kamada Nanao,
Nakamura Yusuke,
Miki Yoshio
Publication year - 1998
Publication title -
genes, chromosomes and cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.754
H-Index - 119
eISSN - 1098-2264
pISSN - 1045-2257
DOI - 10.1002/(sici)1098-2264(199803)21:3<217::aid-gcc5>3.0.co;2-2
Subject(s) - rad51 , biology , brca2 protein , complementary dna , homologous recombination , carcinogenesis , dna , gene , microbiology and biotechnology , dna repair , genetics , mutation , germline mutation
To investigate the biological consequences of aberrant BRCA2 protein during mammary carcinogenesis, we attempted to identify proteins that normally interact with BRCA2. By using a yeast two‐hybrid system with a hybrid protein that contained residues 639–1,508 of BRCA2 protein fused to the GAL4 DNA‐binding domain, we isolated five independent cDNA clones that encoded parts of RAD51 protein, a human homolog of bacterial RecA. In vitro experiments using anti‐RAD51 antibody confirmed interaction of BRCA2 with RAD51. The RAD51‐binding region of BRCA2 detected in the present study was distinct from the region reported recently. Further studies using smaller portions of BRCA2 defined at least two additional RAD51‐binding domains, residues 982–1,066 and 1,139–1,266. Our results suggest that BRCA2 can interact with RAD51 through multiple sites of BRCA2 and that control of mitotic and meiotic recombination and/or of genomic integrity through binding to RAD51 may be a crucial mechanism by which BRCA2 suppresses abnormal proliferation of mammary cells. Genes Chromosomes Cancer 21:217–222, 1998. © 1998 Wiley‐Liss, Inc.