Discovery of an archetypal protein transport system in bacterial outer membranes
Selkrig, Joel, Mosbahi, Khedidja, Webb, Chaille T, Belousoff, Matthew J, Perry, Andrew J, Wells, Timothy J, Morris, Faye, Leyton, Denisse L, Totsika, Makrina, Phan, Minh-Duy, Celik, Nermin, Kelly, Michelle, Oates, Clare, Hartland, Elizabeth L, Robins-Browne, Roy M, Ramarathinam, Sri Harsha, Purcell, Anthony W, Schembri, Mark A, Strugnell, Richard A, Henderson, Ian R, Walker, Daniel, & Lithgow, Trevor (2012) Discovery of an archetypal protein transport system in bacterial outer membranes. Nature Structural & Molecular Biology, 19(5), pp. 506-510.
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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|Item Type:||Journal Article|
|Divisions:||Current > Schools > School of Biomedical Sciences
Current > QUT Faculties and Divisions > Faculty of Health
Current > Institutes > Institute of Health and Biomedical Innovation
|Deposited On:||14 Oct 2014 00:53|
|Last Modified:||16 Oct 2014 00:04|
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