Type I secretion system—it takes three and a substrate
Author(s) -
Kerstin Kanberg,
Olivia Spitz,
Isabelle N. Erenburg,
Tobias Beer,
Lutz Schmitt
Publication year - 2018
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1093/femsle/fny094
Subject(s) - periplasmic space , secretion , bacterial outer membrane , transport protein , virulence , secretory protein , membrane transport protein , microbiology and biotechnology , biology , type vi secretion system , cytosol , inner membrane , membrane protein , biochemistry , membrane , escherichia coli , gene , enzyme
Type I secretion systems are widespread in Gram-negative bacteria and mediate the one-step translocation of a large variety of proteins serving for diverse purposes, including nutrient acquisition or bacterial virulence. Common to most substrates of type I secretion systems is the presence of a C-terminal secretion sequence that is not cleaved during or after translocation. Furthermore, these protein secretion nanomachineries are always composed of an ABC transporter, a membrane fusion protein, both located in the inner bacterial membrane, and a protein of the outer membrane. These three membrane proteins transiently form a 'tunnel channel' across the periplasmic space in the presence of the substrate. Here we summarize the recent findings with respect to structure, function and application of type I secretion systems.
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