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The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations
Open accessAbstract
BACH1 is a nuclear protein that directly interacts with the highly conserved, C-terminal BRCT repeats of the tumor suppressor, BRCA1. Mutations within the BRCT repeats disrupt the interaction between BRCA1 and BACH1, lead to defects in DNA repair, and result in breast and ovarian cancer. BACH1 is necessary for efficient double-strand break repair in a manner that depends on its association with BRCA1. Moreover, some women with early-onset breast cancer and no abnormalities in either BRCA1 or BRCA2 carry germline BACH1 coding sequence changes, suggesting that abnormal BACH1 function contributes to tumor induction. Here, we show that BACH1 is both a DNA-dependent ATPase and a 5′-to-3′ DNA helicase. In two patients with early-onset breast cancer who carry distinct germline BACH1 coding sequence changes, the resulting proteins are defective in helicase activity, indicating that these sequence changes disrupt protein function. These results reinforce the notion that mutant BACH1 participates in breast cancer development.
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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 [56]
In the citing paper
“As predicted, the ATPase and helicase functions were inactivated by a single missense mutation (K52R) in the ATP-binding pocket of the FANCJ helicase domain [56,61,62].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [56]
In the citing paper
“These studies revealed that wild-type FANCJ is a DNA-dependent ATPase, which unwinds DNA in a 5′ to 3′ direction [56].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [56]
In the citing paper
“Consistent with enzyme activity being essential for tumor suppression, the breast cancer-associated mutation in helicase block II (P47A) or an FA-associated mutation in the Fe–S domain (A349P) reduced FANCJ enzyme activity [42,56,63].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [56]
In the citing paper
“The P47A mutant had disrupted enzyme activity”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [56]
In the citing paper
“the M299I mutant had enhanced ATPase, helicase and translocase activity [56,61]”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [56]
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Self-citation
Metadata
- Authors
- Cantor, S., Drapkin, R., Zhang, F., Lin, Y., Han, J., Pamidi, S., & Livingston, D. M.
- Affiliations
- Harvard University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2004-02-17
- Volume
- 101
- Issue
- 8
- Pages
- 2357-2362
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC356955
- OpenAlex
- W2122003098
- Cited by
- 240
- References
- 44
- Citations by year
- 2026: 7 · 2025: 3 · 2024: 4 · 2023: 9 · 2022: 7 · 2021: 11 · 2020: 9 · 2019: 6 · 2018: 5 · 2017: 6 · 2016: 6 · 2015: 10 · 2014: 12 · 2013: 14 · 2012: 13
- FWCI
- 5.80
- Type
- journal article
- Language
- en
- Update notices
- correction (2004-04-27)
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- 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, DNA helicase, DNA-dependent ATPase, germline mutations, early-onset breast cancer, ovarian cancer, DNA double-strand break repair, DNA repair, protein-protein interaction, hereditary cancer predisposition
- MeSH terms
- Adenosine Triphosphatases, DNA Helicases, Humans, Nuclear Proteins, Transcription Factors, Mutagenesis, Site-Directed, Leucine Zippers, Germ-Line Mutation, BRCA1 Protein, Amino Acid Substitution, Basic-Leucine Zipper Transcription Factors, Fanconi Anemia Complementation Group Proteins
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