Site-2 proteases in prokaryotes: regulated intramembrane proteolysis expands to microbial pathogenesis Journal Article
| Authors: | Makinoshima, H.; Glickman, M. S. |
| Article Title: | Site-2 proteases in prokaryotes: regulated intramembrane proteolysis expands to microbial pathogenesis |
| Abstract: | Regulated intramembrane proteolysis (RIP) is a widely distributed mechanism of signal transduction in which membrane-bound proteases cleave transmembrane domains of substrate proteins. The site-2 protease (S2P) class of RIP metalloproteases is present in most bacterial genomes but is generally of unknown function except for the well-characterized proteases RseP and SpoIVFB. In this review we will discuss the biochemical functions and physiologic roles of S2P proteases in bacteria and highlight recent data implicating S2P family members in host-pathogen interactions. © 2006 Elsevier SAS. All rights reserved. |
| Keywords: | signal transduction; promoter region; pathogenesis; nonhuman; chemical analysis; protein domain; protein function; protein degradation; membrane proteins; gene function; enzyme activity; enzyme substrate; bacterial virulence; bacteria (microorganisms); bacterial protein; mycobacterium tuberculosis; bacterial proteins; regulatory mechanism; cell membrane; short survey; proteinase; bacterial genome; protein family; enzyme specificity; regulated intramembrane proteolysis; bacillus subtilis; endopeptidases; bacteria; bacterial enzyme; vibrio cholerae; prokaryote; prokaryota; virulence factors; enterococcus faecalis; lipid regulation; membrane zinc metalloprotease; microbial pathogenesis; site-2 protease; sterol regulatory element binding protein; caulobacter crescentus; enzymatic degradation |
| Journal Title: | Microbes and Infection |
| Volume: | 8 |
| Issue: | 7 |
| ISSN: | 1286-4579 |
| Publisher: | Elsevier Inc. |
| Date Published: | 2006-06-01 |
| Start Page: | 1882 |
| End Page: | 1888 |
| Language: | English |
| DOI: | 10.1016/j.micinf.2006.02.021 |
| PUBMED: | 16731018 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 27" - "Export Date: 4 June 2012" - "CODEN: MCINF" - "Source: Scopus" |
