Literature DB >> 11301010

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

S B Cantor1, 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.   

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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Year:  2001        PMID: 11301010     DOI: 10.1016/s0092-8674(01)00304-x

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  282 in total

1.  HapScope: a software system for automated and visual analysis of functionally annotated haplotypes.

Authors:  Jinghui Zhang; William L Rowe; Jeffery P Struewing; Kenneth H Buetow
Journal:  Nucleic Acids Res       Date:  2002-12-01       Impact factor: 16.971

2.  A subset of ATM- and ATR-dependent phosphorylation events requires the BRCA1 protein.

Authors:  Nicolas Foray; Didier Marot; Anastasia Gabriel; Voahangy Randrianarison; Antony M Carr; Michel Perricaudet; Alan Ashworth; Penny Jeggo
Journal:  EMBO J       Date:  2003-06-02       Impact factor: 11.598

3.  Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains.

Authors:  Maria Victoria E Botuyan; Yves Nominé; Xiaochun Yu; Nenad Juranic; Slobodan Macura; Junjie Chen; Georges Mer
Journal:  Structure       Date:  2004-07       Impact factor: 5.006

4.  Molecular basis of BACH1/FANCJ recognition by TopBP1 in DNA replication checkpoint control.

Authors:  Charles Chung Yun Leung; Zihua Gong; Junjie Chen; J N Mark Glover
Journal:  J Biol Chem       Date:  2010-12-02       Impact factor: 5.157

5.  DNA crosslinking damage and cancer - a tale of friend and foe.

Authors:  Yaling Huang; Lei Li
Journal:  Transl Cancer Res       Date:  2013-06       Impact factor: 1.241

Review 6.  Homologous recombination and human health: the roles of BRCA1, BRCA2, and associated proteins.

Authors:  Rohit Prakash; Yu Zhang; Weiran Feng; Maria Jasin
Journal:  Cold Spring Harb Perspect Biol       Date:  2015-04-01       Impact factor: 10.005

7.  Targeting the FANCJ-BRCA1 interaction promotes a switch from recombination to poleta-dependent bypass.

Authors:  J Xie; R Litman; S Wang; M Peng; S Guillemette; T Rooney; S B Cantor
Journal:  Oncogene       Date:  2010-02-22       Impact factor: 9.867

8.  Redox control of the DNA damage-inducible protein DinG helicase activity via its iron-sulfur cluster.

Authors:  Binbin Ren; Xuewu Duan; Huangen Ding
Journal:  J Biol Chem       Date:  2008-12-12       Impact factor: 5.157

9.  BRCA1 and FancJ cooperatively promote interstrand crosslinker induced centrosome amplification through the activation of polo-like kinase 1.

Authors:  Jianqiu Zou; Deli Zhang; Guang Qin; Xiangming Chen; Hongmin Wang; Dong Zhang
Journal:  Cell Cycle       Date:  2014       Impact factor: 4.534

10.  Structural evidence for direct interactions between the BRCT domains of human BRCA1 and a phospho-peptide from human ACC1.

Authors:  Yang Shen; Liang Tong
Journal:  Biochemistry       Date:  2008-05-02       Impact factor: 3.162

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