Discovery of an archetypal protein transport system in bacterial outer membranes

Research output: Contribution to journalArticle

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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.

In: Nature Structural and Molecular Biology, Vol. 19, No. 5, 2012, p. 506-10, S1.

Research output: Contribution to journalArticle

Harvard

Selkrig, J, Mosbahi, K, Webb, CT, Belousoff, MJ, Perry, AJ, Wells, TJ, Morris, F, Leyton, DL, Totsika, M, Phan, M-D, Celik, N, Kelly, M, Oates, C, Hartland, EL, Robins-Browne, RM, Ramarathinam, SH, Purcell, AW, Schembri, MA, Strugnell, RA, Henderson, IR, Walker, D & Lithgow, T 2012, 'Discovery of an archetypal protein transport system in bacterial outer membranes', Nature Structural and Molecular Biology, vol. 19, no. 5, pp. 506-10, S1. https://doi.org/10.1038/nsmb.2261

APA

Selkrig, J., Mosbahi, K., Webb, C. T., Belousoff, M. J., Perry, A. J., Wells, T. J., Morris, F., Leyton, D. L., Totsika, M., Phan, M-D., Celik, N., Kelly, M., Oates, C., Hartland, E. L., Robins-Browne, R. M., Ramarathinam, S. H., Purcell, A. W., Schembri, M. A., Strugnell, R. A., ... Lithgow, T. (2012). Discovery of an archetypal protein transport system in bacterial outer membranes. Nature Structural and Molecular Biology, 19(5), 506-10, S1. https://doi.org/10.1038/nsmb.2261

Vancouver

Author

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. / Discovery of an archetypal protein transport system in bacterial outer membranes. In: Nature Structural and Molecular Biology. 2012 ; Vol. 19, No. 5. pp. 506-10, S1.

Bibtex

@article{5fee93c951a5422793d2d96d9ff31f5a,
title = "Discovery of an archetypal protein transport system in bacterial outer membranes",
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.",
author = "Joel Selkrig and Khedidja Mosbahi and Webb, {Chaille T} and Belousoff, {Matthew J} and Perry, {Andrew J} and Wells, {Timothy J} and Faye Morris and Leyton, {Denisse L} and Makrina Totsika and Minh-Duy Phan and Nermin Celik and Michelle Kelly and Clare Oates and Hartland, {Elizabeth L} and Robins-Browne, {Roy M} and Ramarathinam, {Sri Harsha} and Purcell, {Anthony W} and Schembri, {Mark A} and Strugnell, {Richard A} and Henderson, {Ian R} and Daniel Walker and Trevor Lithgow",
year = "2012",
doi = "10.1038/nsmb.2261",
language = "English",
volume = "19",
pages = "506--10, S1",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "Nature Publishing Group",
number = "5",

}

RIS

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

Y1 - 2012

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.

U2 - 10.1038/nsmb.2261

DO - 10.1038/nsmb.2261

M3 - Article

C2 - 22466966

VL - 19

SP - 506-10, S1

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 5

ER -