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http://purl.uniprot.org/citations/11931773http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11931773http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11931773http://www.w3.org/2000/01/rdf-schema#comment"In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. The mechanism by which these machines specifically recognize substrates remains unclear. Here, we report the identification of a ClpA cofactor from Escherichia coli, ClpS, which directly influences the ClpAP machine by binding to the N-terminal domain of the chaperone ClpA. The degradation of ClpAP substrates, both SsrA-tagged proteins and ClpA itself, is specifically inhibited by ClpS. In contrast, ClpS enhanced ClpA recognition of two heat-aggregated proteins in vitro and, consequently, the ClpAP-mediated disaggregation and degradation of these substrates. We conclude that ClpS modifies ClpA substrate specificity, potentially redirecting degradation by ClpAP toward aggregated proteins."xsd:string
http://purl.uniprot.org/citations/11931773http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(02)00485-9"xsd:string
http://purl.uniprot.org/citations/11931773http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(02)00485-9"xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/author"Horwich A.L."xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/author"Horwich A.L."xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/author"Bukau B."xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/author"Bukau B."xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/author"Dougan D.A."xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/author"Dougan D.A."xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/author"Reid B.G."xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/author"Reid B.G."xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/pages"673-683"xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/pages"673-683"xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/title"ClpS, a substrate modulator of the ClpAP machine."xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/title"ClpS, a substrate modulator of the ClpAP machine."xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/11931773http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/11931773http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11931773
http://purl.uniprot.org/citations/11931773http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11931773