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BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function.
Cantor, S B; Bell, D W; Ganesan, S; Kass, E M; Drapkin, R; Grossman, S; Wahrer, D C; Sgroi, D C; Lane, W S; Haber, D A; Livingston, D M.
Afiliación
  • Cantor SB; The Dana-Farber Cancer Institute and the Harvard, Medical School, Boston, MA 02115, USA.
Cell ; 105(1): 149-60, 2001 Apr 06.
Article en En | MEDLINE | ID: mdl-11301010
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.
Asunto(s)
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Colección: 01-internacional Asunto principal: Neoplasias de la Mama / ADN Helicasas / Proteína BRCA1 / ARN Helicasas / Proteínas de Unión al ADN / Reparación del ADN Límite: Adult / Female / Humans País/Región como asunto: America do norte Idioma: En Revista: Cell Año: 2001 Tipo del documento: Article País de afiliación: Estados Unidos
Buscar en Google
Colección: 01-internacional Asunto principal: Neoplasias de la Mama / ADN Helicasas / Proteína BRCA1 / ARN Helicasas / Proteínas de Unión al ADN / Reparación del ADN Límite: Adult / Female / Humans País/Región como asunto: America do norte Idioma: En Revista: Cell Año: 2001 Tipo del documento: Article País de afiliación: Estados Unidos