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    Cell. 2001 Apr 6;105(1):149-60.

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

    Cantor SB, Bell DW, Ganesan S, Kass EM, Drapkin R, Grossman S, Wahrer DC, Sgroi DC, Lane WS, Haber DA, Livingston DM.

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    The Dana-Farber Cancer Institute and the Harvard, Medical School, Boston, MA 02115, USA.

    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.

    PMID:
    11301010
    [PubMed - indexed for MEDLINE]

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