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

Sharon B. Cantor, Daphne W. Bell, Shridar Ganesan, Elizabeth M. Kass, Ronny Drapkin, Steven Grossman, Doke C.R. Wahrer, Dennis C. Sgroi, William S. Lane, Daniel A. Haber, David M. Livingston

Research output: Contribution to journalArticle

472 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)149-160
Number of pages12
JournalCell
Volume105
Issue number1
DOIs
StatePublished - Apr 6 2001

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DNA Repair
Repair
Bearings (structural)
Mutation
Germ-Line Mutation
DNA
Proteins
Breast Neoplasms
Derivatives
Neoplasms

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Cantor, S. B., Bell, D. W., Ganesan, S., Kass, E. M., Drapkin, R., Grossman, S., ... Livingston, D. M. (2001). BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function. Cell, 105(1), 149-160. https://doi.org/10.1016/S0092-8674(01)00304-X
Cantor, Sharon B. ; Bell, Daphne W. ; Ganesan, Shridar ; Kass, Elizabeth M. ; Drapkin, Ronny ; Grossman, Steven ; Wahrer, Doke C.R. ; Sgroi, Dennis C. ; Lane, William S. ; Haber, Daniel A. ; Livingston, David M. / BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function. In: Cell. 2001 ; Vol. 105, No. 1. pp. 149-160.
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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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Cantor, SB, Bell, DW, Ganesan, S, Kass, EM, Drapkin, R, Grossman, S, Wahrer, DCR, Sgroi, DC, Lane, WS, Haber, DA & Livingston, DM 2001, 'BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function', Cell, vol. 105, no. 1, pp. 149-160. https://doi.org/10.1016/S0092-8674(01)00304-X

BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function. / Cantor, Sharon B.; Bell, Daphne W.; Ganesan, Shridar; Kass, Elizabeth M.; Drapkin, Ronny; Grossman, Steven; Wahrer, Doke C.R.; Sgroi, Dennis C.; Lane, William S.; Haber, Daniel A.; Livingston, David M.

In: Cell, Vol. 105, No. 1, 06.04.2001, p. 149-160.

Research output: Contribution to journalArticle

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AU - Cantor, Sharon B.

AU - Bell, Daphne W.

AU - Ganesan, Shridar

AU - Kass, Elizabeth M.

AU - Drapkin, Ronny

AU - Grossman, Steven

AU - Wahrer, Doke C.R.

AU - Sgroi, Dennis C.

AU - Lane, William S.

AU - Haber, Daniel A.

AU - Livingston, David M.

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AB - 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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