Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.

The Type II Secretion System (T2SS) is a molecular machine that drives the secretion of fully-folded protein substrates across the bacterial outer membrane. A key element in the machinery is the secretin: an integral, multimeric outer membrane protein that forms the secretion pore. We show that thre...

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Autores principales:	Rhys A Dunstan, Eva Heinz, Lakshmi C Wijeyewickrema, Robert N Pike, Anthony W Purcell, Timothy J Evans, Judyta Praszkier, Roy M Robins-Browne, Richard A Strugnell, Konstantin V Korotkov, Trevor Lithgow
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/921ab55585324c6da9ceed963021e5c1
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spelling	oai:doaj.org-article:921ab55585324c6da9ceed963021e5c12021-11-18T06:06:10ZAssembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.1553-73661553-737410.1371/journal.ppat.1003117https://doaj.org/article/921ab55585324c6da9ceed963021e5c12013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23326233/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The Type II Secretion System (T2SS) is a molecular machine that drives the secretion of fully-folded protein substrates across the bacterial outer membrane. A key element in the machinery is the secretin: an integral, multimeric outer membrane protein that forms the secretion pore. We show that three distinct forms of T2SSs can be distinguished based on the sequence characteristics of their secretin pores. Detailed comparative analysis of two of these, the Klebsiella-type and Vibrio-type, showed them to be further distinguished by the pilotin that mediates their transport and assembly into the outer membrane. We have determined the crystal structure of the novel pilotin AspS from Vibrio cholerae, demonstrating convergent evolution wherein AspS is functionally equivalent and yet structurally unrelated to the pilotins found in Klebsiella and other bacteria. AspS binds to a specific targeting sequence in the Vibrio-type secretins, enhances the kinetics of secretin assembly, and homologs of AspS are found in all species of Vibrio as well those few strains of Escherichia and Shigella that have acquired a Vibrio-type T2SS.Rhys A DunstanEva HeinzLakshmi C WijeyewickremaRobert N PikeAnthony W PurcellTimothy J EvansJudyta PraszkierRoy M Robins-BrowneRichard A StrugnellKonstantin V KorotkovTrevor LithgowPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 9, Iss 1, p e1003117 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Rhys A Dunstan Eva Heinz Lakshmi C Wijeyewickrema Robert N Pike Anthony W Purcell Timothy J Evans Judyta Praszkier Roy M Robins-Browne Richard A Strugnell Konstantin V Korotkov Trevor Lithgow Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.
description	The Type II Secretion System (T2SS) is a molecular machine that drives the secretion of fully-folded protein substrates across the bacterial outer membrane. A key element in the machinery is the secretin: an integral, multimeric outer membrane protein that forms the secretion pore. We show that three distinct forms of T2SSs can be distinguished based on the sequence characteristics of their secretin pores. Detailed comparative analysis of two of these, the Klebsiella-type and Vibrio-type, showed them to be further distinguished by the pilotin that mediates their transport and assembly into the outer membrane. We have determined the crystal structure of the novel pilotin AspS from Vibrio cholerae, demonstrating convergent evolution wherein AspS is functionally equivalent and yet structurally unrelated to the pilotins found in Klebsiella and other bacteria. AspS binds to a specific targeting sequence in the Vibrio-type secretins, enhances the kinetics of secretin assembly, and homologs of AspS are found in all species of Vibrio as well those few strains of Escherichia and Shigella that have acquired a Vibrio-type T2SS.
format	article
author	Rhys A Dunstan Eva Heinz Lakshmi C Wijeyewickrema Robert N Pike Anthony W Purcell Timothy J Evans Judyta Praszkier Roy M Robins-Browne Richard A Strugnell Konstantin V Korotkov Trevor Lithgow
author_facet	Rhys A Dunstan Eva Heinz Lakshmi C Wijeyewickrema Robert N Pike Anthony W Purcell Timothy J Evans Judyta Praszkier Roy M Robins-Browne Richard A Strugnell Konstantin V Korotkov Trevor Lithgow
author_sort	Rhys A Dunstan
title	Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.
title_short	Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.
title_full	Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.
title_fullStr	Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.
title_full_unstemmed	Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.
title_sort	assembly of the type ii secretion system such as found in vibrio cholerae depends on the novel pilotin asps.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/921ab55585324c6da9ceed963021e5c1
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Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.

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