Abstract:
: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.
journal_name
Celljournal_title
Cellauthors
Cantor SB,Bell DW,Ganesan S,Kass EM,Drapkin R,Grossman S,Wahrer DC,Sgroi DC,Lane WS,Haber DA,Livingston DMdoi
10.1016/s0092-8674(01)00304-xsubject
Has Abstractpub_date
2001-04-06 00:00:00pages
149-60issue
1eissn
0092-8674issn
1097-4172pii
S0092-8674(01)00304-Xjournal_volume
105pub_type
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