Title
BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function
UMMS Affiliation
Department of Cancer Biology; Department of Medicine, Division of Hematology/Oncology
Date
4-13-2001
Document Type
Article
Subjects
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 Screening; 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
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.
Rights and Permissions
Citation: Cell. 2001 Apr 6;105(1):149-60.
Related Resources
PubMed ID
11301010
