Identification of ClpP substrates in Caulobacter crescentus reveals a role for regulated proteolysis in bacterial development.

ABSTRACT: Energy-dependent proteases ensure the timely removal of unwanted proteins in a highly selective fashion. In Caulobacter crescentus, protein degradation by the ClpXP protease is critical for cell cycle progression; however, only a handful of substrates are currently known. Here, we use a trapping approach to identify putative substrates of the ClpP associated proteases in C. crescentus. Biochemical validation of several of these targets reveals specific protease recognition motifs and suggests a need for ClpXP-specific degradation beyond degradation of known cell cycle regulators. We focus on a particular instance of regulated proteolysis in Caulobacter by exploring the role of ClpXP in degrading the stalk synthesis transcription factor TacA. We show that TacA degradation is controlled duri

SUBMITTER: Bhat NH 

PROVIDER: S-EPMC3681837 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature