Inhibition of BACH1 (FANCJ) helicase by backbone discontinuity is overcome by increased motor ATPase or length of loading strand
Open accessAbstract
The BRCA1 associated C-terminal helicase (BACH1) associated with breast cancer has been implicated in double strand break (DSB) repair. More recently, BACH1 (FANCJ) has been genetically linked to the chromosomal instability disorder Fanconi Anemia (FA). Understanding the roles of BACH1 in cellular DNA metabolism and how BACH1 dysfunction leads to tumorigenesis requires a comprehensive investigation of its catalytic mechanism and molecular functions in DNA repair. In this study, we have determined that BACH1 helicase contacts with both the translocating and the non-translocating strands of the duplex are critical for its ability to track along the sugar phosphate backbone and unwind dsDNA. An increased motor ATPase of a BACH1 helicase domain variant (M299I) enabled the helicase to unwind the backbone-modified DNA substrate in a more proficient manner. Alternatively, increasing the length of the 5' tail of the DNA substrate allowed BACH1 to overcome the backbone discontinuity, suggesting that BACH1 loading mechanism is critical for its ability to unwind damaged DNA molecules.
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The breast cancer-associated M299I mutant unwound a forked duplex DNA substrate and translocated DNA more robustly than wild-type FANCJ.
“For example, the breast cancer-associated M299I mutant protein unwound a forked duplex DNA substrate and translocated DNA more robustly than wild-type FANCJ (Figure 2) [62,63].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [62]
The ATPase and helicase functions of FANCJ are inactivated by the K52R missense mutation in the ATP-binding pocket.
“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 [62]
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- Authors
- Gupta, R., Sharma, S., Doherty, K. M., Sommers, J. A., Cantor, S. B., & Brosh, R. M.
- Affiliations
- National Institutes of Health (US)
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- Brosh, Robert M.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2006-12
- Volume
- 34
- Issue
- 22
- Pages
- 6673-6683
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC1751539
- OpenAlex
- W1970449119
- Cited by
- 41
- References
- 42
- Citations by year
- 2026: 1 · 2024: 2 · 2023: 1 · 2021: 1 · 2020: 2 · 2017: 2 · 2016: 5 · 2015: 1 · 2014: 1 · 2013: 1 · 2012: 4
- FWCI
- 1.22
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc
- Locations
- Nucleic Acids Research (publishedVersion, cc-by-nc)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship@UMassChan (submittedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- BACH1, helicase mechanism, DNA double-strand break repair, Fanconi anemia, DNA unwinding, DNA damage response
- MeSH terms
- Adenosine Triphosphatases, Amino Acid Sequence, Catalysis, DNA, DNA Helicases, DNA, Single-Stranded, Humans, Molecular Sequence Data, Polymorphism, Genetic, Protein Structure, Tertiary, Basic-Leucine Zipper Transcription Factors, Fanconi Anemia Complementation Group Proteins
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