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http://purl.uniprot.org/citations/9564049http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9564049http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9564049http://www.w3.org/2000/01/rdf-schema#comment"In extracts of human cells, base-base mismatches and small insertion/deletion loops are bound primarily by hMutSalpha, a heterodimer of hMSH2 and hMSH6 (also known as GTBP or p160). Recombinant hMutSalpha bound a G/T mismatch-containing oligonucleotide with an apparent dissociation constant Kd = 2.6 nM, while its affinity for a homoduplex substrate was >20-fold lower. In the presence of ATP, hMutSalpha dissociated from mismatched oligonucleotide substrates, and this reaction was attenuated by mutating the conserved lysine in the ATP-binding domains of hMSH6, hMSH2 or both to arginine. Surprisingly, this reaction required only ATP binding, not hydrolysis. The ATPase activity of hMutSalpha variants carrying the Lys-->Arg mutation in hMSH2 or in hMSH6 was severely affected, but these mutants were still proficient in mismatch binding and were able to complement, albeit to different extents, mismatch repair-deficient cell extracts. The mismatch binding-proficient, ATPase-deficient double mutant was inactive in the complementation assay and its presence in repair-proficient extracts was inhibitory. We conclude that although the ATPase activity of hMutSalpha is dispensible for mismatch binding, it is required for mismatch correction."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.org/dc/terms/identifier"doi:10.1093/emboj/17.9.2677"xsd:string
http://purl.uniprot.org/citations/9564049http://purl.org/dc/terms/identifier"doi:10.1093/emboj/17.9.2677"xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/author"Jiricny J."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/author"Jiricny J."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/author"Palombo F."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/author"Palombo F."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/author"Iaccarino I."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/author"Iaccarino I."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/author"Marra G."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/author"Marra G."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/pages"2677-2686"xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/pages"2677-2686"xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/title"hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/title"hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha."xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/9564049http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/9564049http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9564049
http://purl.uniprot.org/citations/9564049http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9564049