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BACH1, a Novel Helicase-like Protein, Interacts Directly with BRCA1 and Contributes to Its DNA Repair Function
Open accessAbstract
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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“The purified 130-kDa protein was subject to tandem mass spectrometry and the FANCJ gene was cloned and found to consist of 20 exons spanning greater than 180 kb of genomic sequence in chromosome 17q22.”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [8]
In the citing paper
“Furthermore, unlike the classic paradigm for tumor suppressor genes, in which the tumor exclusively lacks the wild-type allele, tumors of individuals who were heterozygous for these two germline FANCJ mutations did not show loss of the corresponding wild-type allele [8].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [8]
In the citing paper
“For example, the P47A variant identified in 2001 [8] and shown to disrupt FANCJ enzyme function [56] was found in the controls of a subsequent study and considered to be unrelated to breast cancer [44].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [8]
In the citing paper
“Among the proteins identified was a protein of approximately 130 kDa that failed to interact with a BRCA1, harboring patient mutations within the BRCT motifs (P1749R and M1775R) [8].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [8]
In the citing paper
“Most notably, the protein product had strong homology to the catalytic and nucleotide-binding domains of other members within the DEAH helicase family, including the xeroderma pigmentosum complimenting group D (XPD) [8].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [8]
In the citing paper
“In keeping with this suggestion, two patients with a family history and early-onset breast cancer were identified that had discrete germline sequence changes, P47A and M299I, targeting the helicase domain of FANCJ [8].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [8]
In the citing paper
“Moreover, the aforementioned P47A mutant had a reduced protein half-life when overexpressed in tissue culture cells [8].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [8]
In the citing paper
“In particular, overexpression of the helicase-inactive K52R mutant in cells with wild-type FANCJ resulted in the accumulation of unrepaired DNA breaks when analyzed by pulse field electrophoresis [8], as well as reduced homologous recombination following double strand break induction [69].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [8]
In the citing paper
“BRCA1 clinical mutations target the BRCT region required for FANCJ binding [8].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [8]
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Metadata
- Authors
- Cantor, S. B., Bell, D. W., Ganesan, S., Kass, E. M., Drapkin, R., Grossman, S., Wahrer, D. C. R., Sgroi, D. C., Lane, W. S., Haber, D. A., & Livingston, D. M.
- Affiliations
- Harvard University (US)
- Massachusetts General Hospital (US)
- Corresponding author
- Livingston, David M.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2001-04
- Volume
- 105
- Issue
- 1
- Pages
- 149-160
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2109173575
- Cited by
- 674
- References
- 61
- Citations by year
- 2026: 17 · 2025: 16 · 2024: 20 · 2023: 25 · 2022: 17 · 2021: 32 · 2020: 23 · 2019: 27 · 2018: 14 · 2017: 20 · 2016: 33 · 2015: 29 · 2014: 24 · 2013: 21 · 2012: 35
- FWCI
- 9.31
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- eScholarship@UMassChan (submittedVersion)
- Funders
- National Heart, Lung, and Blood Institute (T32HL007627, T32-HL07627-16)
- National Cancer Institute (P50 CA 89393, P50CA089393)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › BRCA gene mutations in cancer
- Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
- Keywords
- BACH1, BRCA1, protein-protein interaction, DNA double-strand break repair, homologous recombination, germline mutations, early-onset breast cancer, cancer susceptibility genes
- MeSH terms
- Adult, Binding Sites, Boston, Breast Neoplasms, Cell Line, Chromosomes, Human, Pair 17, DNA Repair, DNA Helicases, DNA-Binding Proteins, Female, Genetic Testing, Humans, Molecular Sequence Data, Protein Binding, Recombinant Fusion Proteins, Transfection, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, Protein Structure, Tertiary, BRCA1 Protein, Genetic Predisposition to Disease, RNA Helicases, Amino Acid Motifs, Spectrometry, Mass, Electrospray Ionization, Fanconi Anemia Complementation Group Proteins
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