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J. Biol. Chem., Vol. 276, Issue 18, 14537-14540, May 4, 2001
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From the Division of Breast and Endocrine Surgery, St. Marianna
University School of Medicine, Kawasaki, 216-8511 Japan
BRCA1-BARD1 constitutes a
heterodimeric RING finger complex associated through its N-terminal
regions. Here we demonstrate that the BRCA1-BARD1 heterodimeric RING
finger complex contains significant ubiquitin ligase activity that can
be disrupted by a breast cancer-derived RING finger mutation in
BRCA1. Whereas individually BRCA1 and BARD1 have very low ubiquitin
ligase activities in vitro, BRCA1 combined with BARD1
exhibits dramatically higher activity. Bacterially purified RING finger
domains comprising residues 1-304 of BRCA1 and residues 25-189 of
BARD1 are capable of polymerizing ubiquitin. The steady-state level of
transfected BRCA1 in vivo was increased by co-transfection
of BARD1, and reciprocally that of transfected BARD1 was increased by
BRCA1 in a dose-dependent manner. The breast cancer-derived
BARD1-interaction-deficient mutant, BRCA1C61G, does not
exhibit ubiquitin ligase activity in vitro. These
results suggest that the BRCA1-BARD1 complex contains a ubiquitin
ligase activity that is important in prevention of breast and ovarian cancer development.
To whom correspondence should be addressed. Tel.: 81-44-977-8111;
Fax: 81-44-976-5964; E-mail: to@marianna-u.ac.jp.
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