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. 2002 Mar;9(3):673-83.
doi: 10.1016/s1097-2765(02)00485-9.

ClpS, a substrate modulator of the ClpAP machine

David A Dougan  1 , Brian G Reid, Arthur L Horwich, Bernd Bukau
Affiliations
Free article

ClpS, a substrate modulator of the ClpAP machine

David A Dougan et al. Mol Cell. 2002 Mar.
Free article

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.

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