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Cantor, SB, Bell, DW, Ganesan, S, Kass, EM, Drapkin, R, Grossman, S, Wahrer, DC, Sgroi, DC, Lane, WS, Haber, DA and Livingston, DM (2001) BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function. Cell 105:149-60
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.
Adult; Amino Acid Motifs/genetics; BRCA1 Protein/metabolism; Binding Sites/physiology; Boston/epidemiology; Breast Neoplasms/epidemiology; Breast Neoplasms/genetics; Cell Line; Chromosomes, Human, Pair 17/genetics; DNA Helicases/genetics; DNA Helicases/metabolism; DNA Repair/genetics; DNA-Binding Proteins; Female; Genetic Predisposition to Disease/genetics; Genetic Testing; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Binding/physiology; Protein Structure, Tertiary/genetics; RNA Helicases/genetics; RNA Helicases/metabolism; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Sequence Homology, Amino Acid; Spectrometry, Mass, Electrospray Ionization; Transfection