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http://purl.uniprot.org/citations/17573527http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17573527http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17573527http://www.w3.org/2000/01/rdf-schema#comment"Msh2-Msh3 and Msh2-Msh6 are two partially redundant mispair-recognition complexes that initiate mismatch repair in eukaryotes. Crystal structures of the prokaryotic homolog MutS suggest the mechanism by which Msh6 interacts with mispairs because key mispair-contacting residues are conserved in these two proteins. Because Msh3 lacks these conserved residues, we constructed a series of mutants to investigate the requirements for mispair interaction by Msh3. We found that a chimeric protein in which the mispair-binding domain (MBD) of Msh6 was replaced by the equivalent domain of Msh3 was functional for mismatch repair. This chimera possessed the mispair-binding specificity of Msh3 and revealed that communication between the MBD and the ATPase domain is conserved between Msh2-Msh3 and Msh2-Msh6. Further, the chimeric protein retained Msh6-like properties with respect to genetic interactions with the MutL homologs and an Msh2 MBD deletion mutant, indicating that Msh3-like behaviors beyond mispair specificity are not features controlled by the MBD."xsd:string
http://purl.uniprot.org/citations/17573527http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0704148104"xsd:string
http://purl.uniprot.org/citations/17573527http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0704148104"xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/author"Putnam C.D."xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/author"Putnam C.D."xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/author"Kolodner R.D."xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/author"Kolodner R.D."xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/author"Shell S.S."xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/author"Shell S.S."xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/pages"10956-10961"xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/pages"10956-10961"xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/title"Chimeric Saccharomyces cerevisiae Msh6 protein with an Msh3 mispair-binding domain combines properties of both proteins."xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/title"Chimeric Saccharomyces cerevisiae Msh6 protein with an Msh3 mispair-binding domain combines properties of both proteins."xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/volume"104"xsd:string
http://purl.uniprot.org/citations/17573527http://purl.uniprot.org/core/volume"104"xsd:string
http://purl.uniprot.org/citations/17573527http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17573527
http://purl.uniprot.org/citations/17573527http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17573527
http://purl.uniprot.org/citations/17573527http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17573527
http://purl.uniprot.org/citations/17573527http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17573527