BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function |
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Authors: | Cantor S B Bell D W Ganesan S Kass E M Drapkin R Grossman S Wahrer D C Sgroi D C Lane W S Haber D A Livingston D M |
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Institution: | The Dana-Farber Cancer Institute and the Harvard, Medical School, Boston, MA 02115, USA. |
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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. |
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