Discovery of an archetypal protein transport system in bacterial outer membranes
Date
2012
Authors
Selkrig, Joel
Mosbahi, Khedidja
Webb, Chaille T
Belousoff, Matthew J
Perry, Andrew J
Wells, Timothy J
Morris, Faye C
Leyton, Denisse
Totsika, Makrina
Phan, Minh-Duy
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Nature Publishing Group
Abstract
Bacteria have mechanisms to export proteins for diverse purposes, including colonization of hosts and pathogenesis. A small number of archetypal bacterial secretion machines have been found in several groups of bacteria and mediate a fundamentally distinct secretion process. Perhaps erroneously, proteins called 'autotransporters' have long been thought to be one of these protein secretion systems. Mounting evidence suggests that autotransporters might be substrates to be secreted, not an autonomous transporter system. We have discovered a new translocation and assembly module (TAM) that promotes efficient secretion of autotransporters in proteobacteria. Functional analysis of the TAM in Citrobacter rodentium, Salmonella enterica and Escherichia coli showed that it consists of an Omp85-family protein, TamA, in the outer membrane and TamB in the inner membrane of diverse bacterial species. The discovery of the TAM provides a new target for the development of therapies to inhibit colonization by bacterial pathogens.
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Keywords
Keywords: outer membrane protein; translocation and assembly module a protein; translocation and assembly module b protein; unclassified drug; article; bacterial outer membrane; Citrobacter rodentium; cluster analysis; Escherichia coli; nonhuman; priority journal;
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Nature Structural and Molecular Biology
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Journal article
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2037-12-31
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