PMID:11931773

Citation	Dougan, DA, Reid, BG, Horwich, AL and Bukau, B (2002) ClpS, a substrate modulator of the ClpAP machine. Mol. Cell 9:673-83
Abstract	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.
Links	PubMed
Keywords	Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Carrier Proteins/genetics; Carrier Proteins/metabolism; Endopeptidase Clp; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Hot Temperature; Luciferases/metabolism; Malate Dehydrogenase/metabolism; Molecular Sequence Data; Operon/genetics; Protein Binding; RNA, Bacterial/metabolism; Sequence Alignment; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism; Substrate Specificity
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