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pubmed-article:9428517pubmed:abstractTextClpX, a molecular chaperone and the regulatory subunit of the ClpXP protease, is shown to contain tandem modular domains that bind to the C-terminal sequences of target proteins in a manner that parallels functional specificity. Nuclear magnetic resonance studies show that these C-terminal sequences are displayed as disordered peptides on the surface of otherwise folded proteins. The ClpX substrate-binding domains are homologous to sequences in other Clp/Hsp100 proteins and are related more distantly to PDZ domains, which also mediate C-terminal specific protein-protein interactions. Conservation of these binding domains indicates that the mode of substrate recognition characterized here for ClpX will be a conserved feature among Clp/Hsp100 family members and a distinguishing characteristic between this chaperone family and the Hsp70 chaperones.lld:pubmed
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pubmed-article:9428517pubmed:articleTitlePDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits.lld:pubmed
pubmed-article:9428517pubmed:affiliationDepartment of Biology, Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge 02139, USA.lld:pubmed
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