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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


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



Publication Data

April 6, 2001

Associated Grants

  • Agency: NCI NIH HHS, Id: P50 CA89393
  • Agency: NHLBI NIH HHS, Id: T32 HL07627-16

Mesh Terms

  • 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