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Biochim Biophys Acta

Title:		Function of site-2 proteases in bacteria and bacterial pathogens
Author(s):		Schneider JS; Glickman MS;
Address:		"Immunology Program, Memorial Sloan Kettering Cancer Center, 1275 York Ave., New York, NY 10065, USA; Program in Immunology and Microbial Pathogenesis, Weill Cornell Graduate School of Biomedical Sciences, USA"
Journal Title:		Biochim Biophys Acta
Year:		2013
Volume:		1828
Issue:		12
Page Number:		2808 - 2814
DOI:		10.1016/j.bbamem.2013.04.019
ISSN/ISBN:		0006-3002 (Print) 0006-3002 (Linking)
Abstract:		"Site-2 proteases (S2Ps) are a class of intramembrane metalloproteases named after the founding member of this protein family, human S2P, which control cholesterol and fatty acid biosynthesis by cleaving Sterol Regulatory Element Binding Proteins which control cholesterol and fatty acid biosynthesis. S2Ps are widely distributed in bacteria and participate in diverse pathways that control such diverse functions as membrane integrity, sporulation, lipid biosynthesis, pheromone production, virulence, and others. The most common signaling mechanism mediated by S2Ps is the coupled degradation of transmembrane anti-Sigma factors to activate ECF Sigma factor regulons. However, additional signaling mechanisms continue to emerge as more prokaryotic S2Ps are characterized, including direct proteolysis of membrane embedded transcription factors and proteolysis of non-transcriptional membrane proteins or membrane protein remnants. In this review we seek to comprehensively review the functions of S2Ps in bacteria and bacterial pathogens and attempt to organize these proteases into conceptual groups that will spur further study. This article is part of a Special Issue entitled: Intramembrane Proteases"
Keywords:		"Bacterial Proteins/classification/genetics/*metabolism *Gene Expression Regulation, Bacterial Gram-Negative Bacteria/*enzymology/genetics/pathogenicity Gram-Positive Bacteria/*enzymology/genetics/pathogenicity Lipid Metabolism Membrane Proteins/classifica;"
Notes:		"MedlineSchneider, Jessica S Glickman, Michael S eng R01 AI080628/AI/NIAID NIH HHS/ T32 AI007621/AI/NIAID NIH HHS/ Review Netherlands 2013/10/09 Biochim Biophys Acta. 2013 Dec; 1828(12):2808-14. doi: 10.1016/j.bbamem.2013.04.019"