TY - JOUR
T1 - Discovery of an archetypal protein transport system in bacterial outer membranes
AU - Selkrig, Joel
AU - Mosbahi, Khedidja
AU - Webb, Chaille T.
AU - Belousoff, Matthew J.
AU - Perry, Andrew J.
AU - Wells, Timothy J.
AU - Morris, Faye
AU - Leyton, Denisse L.
AU - Totsika, Makrina
AU - Phan, Minh Duy
AU - Celik, Nermin
AU - Kelly, Michelle
AU - Oates, Clare
AU - Hartland, Elizabeth L.
AU - Robins-Browne, Roy M.
AU - Ramarathinam, Sri Harsha
AU - Purcell, Anthony W.
AU - Schembri, Mark A.
AU - Strugnell, Richard A.
AU - Henderson, Ian R.
AU - Walker, Daniel
AU - Lithgow, Trevor
PY - 2012/5
Y1 - 2012/5
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84860719904&partnerID=8YFLogxK
U2 - 10.1038/nsmb.2261
DO - 10.1038/nsmb.2261
M3 - Article
SN - 1545-9993
VL - 19
SP - 506
EP - 510
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
IS - 5
ER -