BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function.
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.
Pubmed ID: 11301010 RIS Download
Adult | Amino Acid Motifs | BRCA1 Protein | Binding Sites | Boston | Breast Neoplasms | Cell Line | Chromosomes, Human, Pair 17 | DNA Helicases | DNA Repair | DNA-Binding Proteins | Female | Genetic Predisposition to Disease | Genetic Testing | Humans | Molecular Sequence Data | Mutagenesis, Site-Directed | Protein Binding | Protein Structure, Tertiary | RNA Helicases | Recombinant Fusion Proteins | Sequence Homology, Amino Acid | Spectrometry, Mass, Electrospray Ionization | Transfection