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http://purl.uniprot.org/citations/23999858http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23999858http://www.w3.org/2000/01/rdf-schema#comment"The FANCM/FAAP24 heterodimer has distinct functions in protecting cells from complex DNA lesions such as interstrand crosslinks. These functions rely on the biochemical activity of FANCM/FAAP24 to recognize and bind to damaged DNA or stalled replication forks. However, the DNA-binding activity of this complex was not clearly defined. We investigated how FAAP24 contributes to the DNA-interacting functions of the FANCM/FAAP24 complex by acquiring the N-terminal and C-terminal solution structures of human FAAP24. Modeling of the FAAP24 structure indicates that FAAP24 may possess a high affinity toward single-stranded DNA (ssDNA). Testing of various FAAP24 mutations in vitro and in vivo validated this prediction derived from structural analyses. We found that the DNA-binding and FANCM-interacting functions of FAAP24, although both require the C-terminal (HhH)2 domain, can be distinguished by segregation-of-function mutations. These results demonstrate dual roles of FAAP24 in DNA damage response against crosslinking lesions, one through the formation of FANCM/FAAP24 heterodimer and the other via its ssDNA-binding activity required in optimized checkpoint activation."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.org/dc/terms/identifier"doi:10.1038/cr.2013.124"xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/author"Gong W."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/author"Han X."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/author"Li L."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/author"Wu F."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/author"Shi C."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/author"Tian C."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/author"Do H."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/author"Leung J.W."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/author"Lowery M.G."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/name"Cell Res"xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/pages"1215-1228"xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/title"Structure analysis of FAAP24 reveals single-stranded DNA-binding activity and domain functions in DNA damage response."xsd:string
http://purl.uniprot.org/citations/23999858http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/23999858http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23999858
http://purl.uniprot.org/citations/23999858http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23999858
http://purl.uniprot.org/uniprot/#_A0A0S2Z5V6-mappedCitation-23999858http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23999858
http://purl.uniprot.org/uniprot/#_K7EKQ4-mappedCitation-23999858http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23999858
http://purl.uniprot.org/uniprot/#_Q9BTP7-mappedCitation-23999858http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23999858
http://purl.uniprot.org/uniprot/#_X6R368-mappedCitation-23999858http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23999858