Membrane proteases in the bacterial protein secretion and quality control pathway.
Proteolytic cleavage of proteins that are permanently or transiently associated with the cytoplasmic membrane is crucially important for a wide range of essential processes in bacteria. This applies in particular to the secretion of proteins and to membrane protein quality control. Major progress has been made in elucidating the structure-function relationships of many of the responsible membrane proteases, including signal peptidases, signal peptide hydrolases, FtsH, the rhomboid protease GlpG, and the site 1 protease DegS. These enzymes employ very different mechanisms to cleave substrates at the cytoplasmic and extracytoplasmic membrane surfaces or within the plane of the membrane. This review highlights the different ways that bacterial membrane proteases degrade their substrates, with special emphasis on catalytic mechanisms and substrate delivery to the respective active sites.
Department of Chemistry, The Ohio State University, Columbus, Ohio, USA. dalbey@chemistry.ohio-state.edu
Ross E
RE
Dalbey
Peng
P
Wang
Jan Maarten
JM
van Dijl
D020134:Catalytic Domain; D002462:Cell Membrane / Q000201:enzymology* / Q000378:metabolism; D006867:Hydrolases / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D021382:Protein Sorting Signals; D021381:Protein Transport; D013379:Substrate Specificity
D008565:Membrane Proteins; D021382:Protein Sorting Signals; D006867:Hydrolases; D010447:Peptide Hydrolases