Reduction in adaptor amounts establishes degradation hierarchy among protease substrates.

ABSTRACT: ATP-dependent proteases control critical cellular processes, including development, physiology, and virulence. A given protease may recognize a substrate directly via an unfoldase domain or subunit or indirectly via an adaptor that delivers the substrate to the unfoldase. We now report that cells achieve differential stability among substrates of a given protease by modulating adaptor amounts. We establish that the regulatory protein PhoP represses transcription of the gene specifying the ClpAP protease adaptor ClpS when the bacteria Salmonella enterica and Escherichia coli experience low cytoplasmic Mg²⁺ The resulting decrease in ClpS amounts diminishes proteolysis of several ClpSAP-dependent substrates, including the putrescine aminotransferase Oat, which heighte

SUBMITTER: Yeom J 

PROVIDER: S-EPMC5948988 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature