Function of site-2 proteases in bacteria and bacterial pathogens.
Function of site-2 proteases in bacteria and bacterial pathogens.
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DOI:
10.1016/j.bbamem.2013.04.019
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发表时间:
2013-12
期刊:
影响因子:
--
通讯作者:
Glickman MS
中科院分区:
文献类型:
--
作者:
Schneider JS;Glickman MS
Site-2 Proteases (S2Ps) are a class of intramembrane metalloproteases named after the founding member of this protein family, human S2P, which cleaves 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.