Proteases and their targets in Escherichia coli.
Proteolysis in Escherichia coli serves to rid the cell of abnormal and misfolded proteins and to limit the time and amounts of availability of critical regulatory proteins. Most intracellular proteolysis is initiated by energy-dependent proteases, including Lon, ClpXP, and HflB; HflB is the only essential E. coli protease. The ATPase domains of these proteases mediate substrate recognition. Recognition elements in target are not well defined, but are probably not specific amino acid sequences. Naturally unstable protein substrates include the regulatory sigma factors for heat shock and stationary phase gene expression, sigma 32 and RpoS. Other cellular proteins serve as environmental sensors that modulate the availability of the unstable proteins to the proteases, resulting in rapid changes in sigma factor levels and therefore in gene transcription. Many of the specific proteases found in E. coli are well-conserved in both prokaryotes and eukaryotes, and serve critical functions in developmental systems.
Gottesman
S
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Laboratory of Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892-4255, USA. susang@helix.nih.gov
D010450:Endopeptidases / Q000378:metabolism*; D004734:Energy Metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D005818:Genetic Engineering; D006868:Hydrolysis; D013379:Substrate Specificity
D010450:Endopeptidases