BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function

被引:591
作者
Cantor, SB
Bell, DW
Ganesan, S
Kass, EM
Drapkin, R
Grossman, S
Wahrer, DCR
Sgroi, DC
Lane, WS
Haber, DA
Livingston, DM [1 ]
机构
[1] Dana Farber Canc Inst, Boston, MA 02115 USA
[2] Harvard Univ, Sch Med, Boston, MA 02115 USA
[3] Massachusetts Gen Hosp, Ctr Canc Risk Anal, Charlestown, MA 02129 USA
[4] Massachusetts Gen Hosp, Mol Pathol Unit, Charlestown, MA 02129 USA
[5] Harvard Univ, Microchem & Proteom Anal Facil, Cambridge, MA 02138 USA
关键词
D O I
10.1016/S0092-8674(01)00304-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
BRCA1 interacts in vivo with a novel protein, BACH1, a member of the DEAH helicase family. BACH1 binds directly to the BRCT repeats of BRCA1.A BACH1 derivative, bearing a mutation in a residue that was essential for catalytic function in other helicases, interfered with normal double-strand break repair in a manner that was dependent on its BRCA1 binding function. Thus, BACH1/BRCA1 complex formation contributes to a key BRCA1 activity. In addition, germline BACH1 mutations affecting the helicase domain were detected in two early-onset breast cancer patients and not in 200 matched controls. Thus, it is conceivable that, like BRCA1, BACH1 is a target of germline cancer-inducing mutations.
引用
收藏
页码:149 / 160
页数:12
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