A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2005-09

AUTHORS

Amom Ruhikanta Meetei, Annette L Medhurst, Chen Ling, Yutong Xue, Thiyam Ramsing Singh, Patrick Bier, Jurgen Steltenpool, Stacie Stone, Inderjeet Dokal, Christopher G Mathew, Maureen Hoatlin, Hans Joenje, Johan P de Winter, Weidong Wang

ABSTRACT

Fanconi anemia is a genetic disease characterized by genomic instability and cancer predisposition. Nine genes involved in Fanconi anemia have been identified; their products participate in a DNA damage-response network involving BRCA1 and BRCA2 (refs. 2,3). We previously purified a Fanconi anemia core complex containing the FANCL ubiquitin ligase and six other Fanconi anemia-associated proteins. Each protein in this complex is essential for monoubiquitination of FANCD2, a key reaction in the Fanconi anemia DNA damage-response pathway. Here we show that another component of this complex, FAAP250, is mutant in individuals with Fanconi anemia of a new complementation group (FA-M). FAAP250 or FANCM has sequence similarity to known DNA-repair proteins, including archaeal Hef, yeast MPH1 and human ERCC4 or XPF. FANCM can dissociate DNA triplex, possibly owing to its ability to translocate on duplex DNA. FANCM is essential for monoubiquitination of FANCD2 and becomes hyperphosphorylated in response to DNA damage. Our data suggest an evolutionary link between Fanconi anemia-associated proteins and DNA repair; FANCM may act as an engine that translocates the Fanconi anemia core complex along DNA. More... »

PAGES

958-963

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ng1626

DOI

http://dx.doi.org/10.1038/ng1626

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005559671

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16116422


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