Fanconi anemia group J mutation abolishes its DNA repair function by uncoupling DNA translocation from helicase activity or disruption of protein-DNA complexes
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Fanconi anemia (FA) is a genetic disease characterized by congenital abnormalities, bone marrow failure, and susceptibility to leukemia and other cancers. FANCJ, one of 13 genes linked to FA, encodes a DNA helicase proposed to operate in homologous recombination repair and replicational stress response. The pathogenic FANCJ-A349P amino acid substitution resides immediately adjacent to a highly conserved cysteine of the iron-sulfur domain. Given the genetic linkage of the FANCJ-A349P allele to FA, we investigated the effect of this particular mutation on the biochemical and cellular functions of the FANCJ protein. Purified recombinant FANCJ-A349P protein had reduced iron and was defective in coupling adenosine triphosphate (ATP) hydrolysis and translocase activity to unwinding forked duplex or G-quadruplex DNA substrates or disrupting protein-DNA complexes. The FANCJ-A349P allele failed to rescue cisplatin or telomestatin sensitivity of a FA-J null cell line as detected by cell survival or γ-H2AX foci formation. Furthermore, expression of FANCJ-A349P in a wild-type background exerted a dominant-negative effect, indicating that the mutant protein interferes with normal DNA metabolism. The ability of FANCJ to use the energy from ATP hydrolysis to produce the force required to unwind DNA or destabilize protein bound to DNA is required for its role in DNA repair.
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Cancer in patients carrying P47A or M299I may have involved a dominant negative effect of the mutant FANCJ proteins.
“Thus, cancer in these patients may have been related to the dominant negative effect of these mutant FANCJ proteins.”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [42]
The P47A mutant is enzymatically inactive in vitro, similar to K52R or A349P, which dominantly disrupted DNA repair when expressed in cells.
“Consistent with this idea, the P47A mutant is enzyme inactive in vitro, similar to the helicace-inactive FANCJ mutant species, K52R, or FA-associated A349P, which dominantly disrupted DNA repair when expressed in cells [41,42].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [42]
Experiments using FANCJ-null FA-J patient cells complemented with K52R or A349P demonstrated that FANCJ enzyme activity and the Fe-S domain are essential for DNA interstrand crosslink repair.
“Experiments using FANCJ-null FA-J patient cells complemented with K52R or the A349P FA-associated mutant demonstrated that FANCJ enzyme activity and the Fe–S domain are essential for DNA interstrand crosslink repair [42,73].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [42]
The breast cancer-associated P47A mutation and the FA-associated A349P mutation reduce FANCJ enzyme activity.
“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 [42]
FA-J patient cells accumulate deletions in regions containing G4-DNA, and recombinant FANCJ A349P fails to unwind G4-DNA substrates.
“In support of this function, FA-J patient cells accumulate deletions in regions containing G4-DNA, and the recombinant FANCJ A349P mutant protein fails to unwind G4-DNA substrates [42,79].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [42]
The A349P mutant retained some DNA unwinding activity on a set of substrates but could not couple ATP hydrolysis to unwinding forked duplex structures or DNA translocation.
“Interestingly, the A349P mutant protein retained some DNA unwinding activity on a set of DNA substrates, but was unable to couple ATP hydrolysis with the enzyme activity necessary to unwind forked duplex structures or translocate DNA [42].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [42]
Expression of A349P in cells with wild-type FANCJ had a dominant negative effect, enhancing sensitivity to the G4-DNA binding compound telomestatin.
“In fact, expression of A349P in cells with wild-type FANCJ had a dominant negative effect, enhancing sensitivity to the G4-DNA binding compound telomestatin [42].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [42]
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Self-citationGetting Ready for the Dance: FANCJ Irons Out DNA Wrinkles
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Self-citationFancJ/Brip1 helicase protects against genomic losses and gains in vertebrate cells
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Self-citationThe phenotype of FancB-mutant mouse embryonic stem cells
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Mutational analysis of FANCJ helicase
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Self-citationBLM’s balancing act and the involvement of FANCJ in DNA repair
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Guardians of the Genome: Iron–Sulfur Proteins in the Nucleus
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Screening for mutations in two exons of FANCG gene in Pakistani population
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Self-citationHow DNA secondary structures drive replication fork instability
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Loss of Mitochondrial Localization of Human FANCG Causes Defective FANCJ Helicase
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Cellular Assays to Study the Functional Importance of Human DNA Repair Helicases
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Self-citationA DNA helicase remodeling proteins: How DNA-protein crosslink repair unfolds via FANCJ
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Chronic Oxidative Stress Leads to Genomic Instability in the Pathogenesis of Fanconi Anemia
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Purification and biochemical characterization of the G4 resolvase and DNA helicase FANCJ
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SURVEY AND SUMMARY DNA helicase and helicase–nuclease enzymes with a conserved iron–sulfur cluster
Wu, Y., & Brosh, R. M. (2011)
Self-citationData from Rare BRIP1 Missense Alleles Confer Risk for Ovarian and Breast Cancer
Moyer, C. L., Ivanovich, J. L., Gillespie, J. L., Doberstein, R., Radke, M. R., Richardson, M. E., Kaufmann, S. H., Swisher, E. M., & Goodfellow, P. J. (2023) · doi:10.1158/0008-5472.c.6511902.v1
Data from Rare BRIP1 Missense Alleles Confer Risk for Ovarian and Breast Cancer
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- Authors
- Wu, Y., Sommers, J. A., Suhasini, A. N., Leonard, T., Deakyne, J. S., Mazin, A. V., Shin-ya, K., Kitao, H., & Brosh, R. M.
- Affiliations
- National Institutes of Health (US)
- Drexel University (US)
- National Institute of Advanced Industrial Science and Technology, Tokyo, Japan; and
- Kyoto University (JP)
- ORCID
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2010-11-11
- Volume
- 116
- Issue
- 19
- Pages
- 3780-3791
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- PMC
- PMC2981534
- OpenAlex
- W2084751512
- Cited by
- 72
- References
- 41
- Citations by year
- 2025: 1 · 2024: 3 · 2023: 6 · 2022: 3 · 2021: 6 · 2020: 6 · 2019: 5 · 2018: 3 · 2017: 5 · 2016: 6 · 2015: 5 · 2014: 6 · 2013: 3 · 2012: 5
- FWCI
- 2.21
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Blood (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (CA100839, R01CA100839, R56CA100839)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Blood disorders and treatments
- Health Sciences › Medicine › Pathology and Forensic Medicine › Genetic factors in colorectal cancer
- Keywords
- Fanconi anemia, FANCJ, DNA helicase, DNA translocation, ATP hydrolysis, DNA repair, homologous recombination, G-quadruplex, protein-DNA complex, dominant negative effect, cisplatin sensitivity, telomestatin, γH2AX foci
- MeSH terms
- Adenosine Triphosphatases, Adenosine Triphosphate, Amino Acid Sequence, DNA, DNA Repair, DNA Helicases, Humans, Iron, Molecular Sequence Data, Oxazoles, Recombinant Proteins, Mitomycin, Amino Acid Substitution, Mutation, Missense, Mutant Proteins, Basic-Leucine Zipper Transcription Factors, Fanconi Anemia Complementation Group Proteins, Protein Stability, In Vitro Techniques
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