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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adult
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Amino Acid Motifs / genetics
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BRCA1 Protein / metabolism*
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Binding Sites / physiology
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Boston / epidemiology
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Breast Neoplasms / epidemiology
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Breast Neoplasms / genetics*
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Cell Line
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Chromosomes, Human, Pair 17 / genetics
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DNA Helicases / genetics
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DNA Helicases / metabolism*
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DNA Repair / genetics*
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DNA-Binding Proteins*
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Fanconi Anemia Complementation Group Proteins
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Female
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Genetic Predisposition to Disease / genetics
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Genetic Testing
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Humans
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Protein Binding / physiology
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Protein Structure, Tertiary / genetics
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RNA Helicases / genetics
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RNA Helicases / metabolism*
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Sequence Homology, Amino Acid
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Spectrometry, Mass, Electrospray Ionization
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Transfection
Substances
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BRCA1 Protein
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DNA-Binding Proteins
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Fanconi Anemia Complementation Group Proteins
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Recombinant Fusion Proteins
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DNA Helicases
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BRIP1 protein, human
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RNA Helicases