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http://purl.uniprot.org/citations/9380710http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9380710http://www.w3.org/2000/01/rdf-schema#comment"The structural and functional organization of the Cct complex was addressed by genetic analyses of subunit interactions and catalytic cooperativity among five of the eight different essential subunits, Cct1p-Cct8p, in the yeast Saccharomyces cerevisiae. The cct1-1, cct2-3, and cct3-1 alleles, containing mutations at the conserved putative ATP-binding motif, GDGTT, are cold-sensitive, whereas single and multiple replacements of the corresponding motif in Cct6p are well tolerated by the cell. We demonstrated herein that cct6-3 (L19S), but not the parolog cct1-5 (R26I), specifically suppresses the cct1-1, cct2-3, and cct3-1 alleles, and that this suppression can be modulated by mutations in a putative phosphorylation motif, RXS, and the putative ATP-binding pocket of Cct6p. Our results suggest that the Cct ring is comprised of a single hetero-oligomer containing eight subunits of differential functional hierarchy, in which catalytic cooperativity of ATP-binding/hydrolysis takes place in a sequential manner different from the concerted cooperativity proposed for GroEL."xsd:string
http://purl.uniprot.org/citations/9380710http://purl.org/dc/terms/identifier"doi:10.1073/pnas.94.20.10780"xsd:string
http://purl.uniprot.org/citations/9380710http://purl.uniprot.org/core/author"Sherman F."xsd:string
http://purl.uniprot.org/citations/9380710http://purl.uniprot.org/core/author"Lin P."xsd:string
http://purl.uniprot.org/citations/9380710http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9380710http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/9380710http://purl.uniprot.org/core/pages"10780-10785"xsd:string
http://purl.uniprot.org/citations/9380710http://purl.uniprot.org/core/title"The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex."xsd:string
http://purl.uniprot.org/citations/9380710http://purl.uniprot.org/core/volume"94"xsd:string
http://purl.uniprot.org/citations/9380710http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9380710
http://purl.uniprot.org/citations/9380710http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9380710
http://purl.uniprot.org/uniprot/#_P39076-mappedCitation-9380710http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9380710
http://purl.uniprot.org/uniprot/#_P39077-mappedCitation-9380710http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9380710
http://purl.uniprot.org/uniprot/#_P39079-mappedCitation-9380710http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9380710
http://purl.uniprot.org/uniprot/#_P12612-mappedCitation-9380710http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9380710
http://purl.uniprot.org/uniprot/P12612http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9380710
http://purl.uniprot.org/uniprot/P39079http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9380710
http://purl.uniprot.org/uniprot/P39076http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9380710
http://purl.uniprot.org/uniprot/P39077http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9380710