Valine 1532 of human BRC repeat 4 plays an important role in the interaction between BRCA2 and RAD51

Kazuhiko Ochiai, Yasunaga Yoshikawa, Kumiko Yoshimatsu, Toshina Oonuma, Yukiko Tomioka, Eichi Takeda, Jiro Arikawa, Katsumi Mominoki, Toshinori Omi, Kazuyoshi Hashizume, Masami Morimatsu

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

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 languageEnglish
Pages (from-to)1771-1777
Number of pages7
JournalFEBS Letters
Volume585
Issue number12
DOIs
Publication statusPublished - Jun 23 2011

Keywords

  • BRC repeat
  • BRCA2
  • Canine
  • Homologous recombination
  • RAD51

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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