Assembly of the secretion pores GspD, Wza and CsgG into bacterial outer membranes does not require the Omp85 proteins BamA or TamA

Rhys A Dunstan, Iain D Hay, Jonathan J Wilksch, Ralf B Schittenhelm, Anthony W Purcell, Joan Marea Clark, Adam Costin, Georg Ramm, Richard A Strugnell, Trevor J Lithgow

Research output: Contribution to journalArticleResearchpeer-review

29 Citations (Scopus)

Abstract

In Gram-negative bacteria, beta-barrel proteins are integrated into the outer membrane by the beta-barrel assembly machinery, with key components of the machinery being the Omp85 family members BamA and TamA. Recent crystal structures and cryo-electron microscopy show a diverse set of secretion pores in Gram-negative bacteria, with alpha-helix (Wza, GspD) or beta-strand (CsgG) transmembrane segments in the outer membrane. We developed assays to measure the assembly of three distinct secretion pores that mediate protein (GspD), curli fibre (CsgG) and capsular polysaccharide (Wza) secretion by bacteria, and show that depletion of BamA and TamA does not diminish the assembly of Wza, GspD or CsgG. Like the well characterized pilotins for GspD and other secretins, small periplasmic proteins enhance the assembly of the CsgG beta-barrel. We discuss a model for integral protein assembly into the bacterial outer membrane, focusing on the commonalities and differences in the assembly of Wza, GspD and CsgG.
Original languageEnglish
Pages (from-to)616 - 629
Number of pages14
JournalMolecular Microbiology
Volume97
Issue number4
DOIs
Publication statusPublished - 2015

Cite this

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title = "Assembly of the secretion pores GspD, Wza and CsgG into bacterial outer membranes does not require the Omp85 proteins BamA or TamA",
abstract = "In Gram-negative bacteria, beta-barrel proteins are integrated into the outer membrane by the beta-barrel assembly machinery, with key components of the machinery being the Omp85 family members BamA and TamA. Recent crystal structures and cryo-electron microscopy show a diverse set of secretion pores in Gram-negative bacteria, with alpha-helix (Wza, GspD) or beta-strand (CsgG) transmembrane segments in the outer membrane. We developed assays to measure the assembly of three distinct secretion pores that mediate protein (GspD), curli fibre (CsgG) and capsular polysaccharide (Wza) secretion by bacteria, and show that depletion of BamA and TamA does not diminish the assembly of Wza, GspD or CsgG. Like the well characterized pilotins for GspD and other secretins, small periplasmic proteins enhance the assembly of the CsgG beta-barrel. We discuss a model for integral protein assembly into the bacterial outer membrane, focusing on the commonalities and differences in the assembly of Wza, GspD and CsgG.",
author = "Dunstan, {Rhys A} and Hay, {Iain D} and Wilksch, {Jonathan J} and Schittenhelm, {Ralf B} and Purcell, {Anthony W} and Clark, {Joan Marea} and Adam Costin and Georg Ramm and Strugnell, {Richard A} and Lithgow, {Trevor J}",
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language = "English",
volume = "97",
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journal = "Molecular Microbiology",
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Assembly of the secretion pores GspD, Wza and CsgG into bacterial outer membranes does not require the Omp85 proteins BamA or TamA. / Dunstan, Rhys A; Hay, Iain D; Wilksch, Jonathan J; Schittenhelm, Ralf B; Purcell, Anthony W; Clark, Joan Marea; Costin, Adam; Ramm, Georg; Strugnell, Richard A; Lithgow, Trevor J.

In: Molecular Microbiology, Vol. 97, No. 4, 2015, p. 616 - 629.

Research output: Contribution to journalArticleResearchpeer-review

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T1 - Assembly of the secretion pores GspD, Wza and CsgG into bacterial outer membranes does not require the Omp85 proteins BamA or TamA

AU - Dunstan, Rhys A

AU - Hay, Iain D

AU - Wilksch, Jonathan J

AU - Schittenhelm, Ralf B

AU - Purcell, Anthony W

AU - Clark, Joan Marea

AU - Costin, Adam

AU - Ramm, Georg

AU - Strugnell, Richard A

AU - Lithgow, Trevor J

PY - 2015

Y1 - 2015

N2 - In Gram-negative bacteria, beta-barrel proteins are integrated into the outer membrane by the beta-barrel assembly machinery, with key components of the machinery being the Omp85 family members BamA and TamA. Recent crystal structures and cryo-electron microscopy show a diverse set of secretion pores in Gram-negative bacteria, with alpha-helix (Wza, GspD) or beta-strand (CsgG) transmembrane segments in the outer membrane. We developed assays to measure the assembly of three distinct secretion pores that mediate protein (GspD), curli fibre (CsgG) and capsular polysaccharide (Wza) secretion by bacteria, and show that depletion of BamA and TamA does not diminish the assembly of Wza, GspD or CsgG. Like the well characterized pilotins for GspD and other secretins, small periplasmic proteins enhance the assembly of the CsgG beta-barrel. We discuss a model for integral protein assembly into the bacterial outer membrane, focusing on the commonalities and differences in the assembly of Wza, GspD and CsgG.

AB - In Gram-negative bacteria, beta-barrel proteins are integrated into the outer membrane by the beta-barrel assembly machinery, with key components of the machinery being the Omp85 family members BamA and TamA. Recent crystal structures and cryo-electron microscopy show a diverse set of secretion pores in Gram-negative bacteria, with alpha-helix (Wza, GspD) or beta-strand (CsgG) transmembrane segments in the outer membrane. We developed assays to measure the assembly of three distinct secretion pores that mediate protein (GspD), curli fibre (CsgG) and capsular polysaccharide (Wza) secretion by bacteria, and show that depletion of BamA and TamA does not diminish the assembly of Wza, GspD or CsgG. Like the well characterized pilotins for GspD and other secretins, small periplasmic proteins enhance the assembly of the CsgG beta-barrel. We discuss a model for integral protein assembly into the bacterial outer membrane, focusing on the commonalities and differences in the assembly of Wza, GspD and CsgG.

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