Events that stall bacterial protein, synthesis activate the ssrA-tagging ma
chinery, resulting in resumption of translation and addition of an 11-resid
ue peptide to the carboxyl terminus of the nascent chain. This ssrA-encoded
peptide tag marks the incomplete protein for degradation by the energy-dep
endent ClpXP protease. Here, a ribosome-associated protein, SspB, was found
to bind specifically to ssrA-tagged proteins and to enhance recognition of
these proteins by ClpXP. Cells with an sspB mutation are defective in degr
ading ssrA-tagged proteins, demonstrating that SspB is a specificity-enhanc
ing factor for ClpXP that controls substrate choice.