Insight into the Roles of Helicase Motif Ia by Characterizing Fanconi Anemia Group J Protein (FANCJ) Patient Mutations

Guo, Mingke; Vidhyasagar, Venkatasubramanian; Ding, Hao; Wu, Yuliang

doi:10.1074/jbc.m113.538892

Cited by 15 publications

(13 citation statements)

References 57 publications

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“…BRIP1 (BRCA1-interacting protein C-terminal helicase 1) is the official gene symbol for FANCJ . Amino-acid substitutions in BRIP1/FANCJ, such as R251C, Q255H, and A349P, were found to be disease-causing [ 32 , 33 ].…”

Section: Genetics Of Fa: Human Fanc Genesmentioning

confidence: 99%

Update of the human and mouse Fanconi anemia genes

Dong¹,

et al. 2015

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Fanconi anemia (FA) is a recessively inherited disease manifesting developmental abnormalities, bone marrow failure, and increased risk of malignancies. Whereas FA has been studied for nearly 90 years, only in the last 20 years have increasing numbers of genes been implicated in the pathogenesis associated with this genetic disease. To date, 19 genes have been identified that encode Fanconi anemia complementation group proteins, all of which are named or aliased, using the root symbol “FANC.” Fanconi anemia subtype (FANC) proteins function in a common DNA repair pathway called “the FA pathway,” which is essential for maintaining genomic integrity. The various FANC mutant proteins contribute to distinct steps associated with FA pathogenesis. Herein, we provide a review update of the 19 human FANC and their mouse orthologs, an evolutionary perspective on the FANC genes, and the functional significance of the FA DNA repair pathway in association with clinical disorders. This is an example of a set of genes––known to exist in vertebrates, invertebrates, plants, and yeast––that are grouped together on the basis of shared biochemical and physiological functions, rather than evolutionary phylogeny, and have been named on this basis by the HUGO Gene Nomenclature Committee (HGNC).

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Section: Genetics Of Fa: Human Fanc Genesmentioning

confidence: 99%

Update of the human and mouse Fanconi anemia genes

Dong¹,

et al. 2015

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“…Two FA patient-derived missense mutations in motif Ia, R251C, and Q255H, were characterized by the Wu lab ( Guo et al, 2014 ; Figure 2 ). Although expression of either R251C or Q255H mutant could not rescue the cisplatin sensitivity of a fancj null cell line, the two mutations exerted markedly different effects on the biochemical functions of FANCJ in vitro .…”

Section: Novel Insights To Fancj Structure-function Relationships By mentioning

confidence: 99%

Molecular and cellular functions of the FANCJ DNA helicase defective in cancer and in Fanconi anemia

Brosh

Cantor

2014

Front. Genet.

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The FANCJ DNA helicase is mutated in hereditary breast and ovarian cancer as well as the progressive bone marrow failure disorder Fanconi anemia (FA). FANCJ is linked to cancer suppression and DNA double strand break repair through its direct interaction with the hereditary breast cancer associated gene product, BRCA1. FANCJ also operates in the FA pathway of interstrand cross-link repair and contributes to homologous recombination. FANCJ collaborates with a number of DNA metabolizing proteins implicated in DNA damage detection and repair, and plays an important role in cell cycle checkpoint control. In addition to its role in the classical FA pathway, FANCJ is believed to have other functions that are centered on alleviating replication stress. FANCJ resolves G-quadruplex (G4) DNA structures that are known to affect cellular replication and transcription, and potentially play a role in the preservation and functionality of chromosomal structures such as telomeres. Recent studies suggest that FANCJ helps to maintain chromatin structure and preserve epigenetic stability by facilitating smooth progression of the replication fork when it encounters DNA damage or an alternate DNA structure such as a G4. Ongoing studies suggest a prominent but still not well-understood role of FANCJ in transcriptional regulation, chromosomal structure and function, and DNA damage repair to maintain genomic stability. This review will synthesize our current understanding of the molecular and cellular functions of FANCJ that are critical for chromosomal integrity.

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“…The concentrations of wild-type and mutant ChlR1 proteins were determined by Bradford (Bio-Rad) using BSA as a standard. FANCJ protein was purified as previously described (40).…”

Section: Methodsmentioning

confidence: 99%

A Distinct Triplex DNA Unwinding Activity of ChlR1 Helicase

Guo

Hundseth

Ding

et al. 2015

Journal of Biological Chemistry

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Background: DNA triplex helix structures are alternate DNA structures that can be a source of genomic instability. Results: ChlR1 helicase has a novel and distinct triplex DNA unwinding activity. Conclusion: ChlR1 defends genome integrity by resolving triplex DNA structures. Significance: The processing of triplex DNA substrates by proteins such as ChlR1 plays critical roles in genome maintenance.

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Insight into the Roles of Helicase Motif Ia by Characterizing Fanconi Anemia Group J Protein (FANCJ) Patient Mutations

Cited by 15 publications

References 57 publications

Update of the human and mouse Fanconi anemia genes

Update of the human and mouse Fanconi anemia genes

Molecular and cellular functions of the FANCJ DNA helicase defective in cancer and in Fanconi anemia

A Distinct Triplex DNA Unwinding Activity of ChlR1 Helicase

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