1. Academic Validation
  2. BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function

BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function

  • Cell. 2001 Apr 6;105(1):149-60. doi: 10.1016/s0092-8674(01)00304-x.
S B Cantor 1 D W Bell S Ganesan E M Kass R Drapkin S Grossman D C Wahrer D C Sgroi W S Lane D A Haber D M Livingston
Affiliations

Affiliation

  • 1 The Dana-Farber Cancer Institute and the Harvard, Medical School, Boston, MA 02115, USA.
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.

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