Systematic dissection of the agrobacterium type VI secretion system reveals machinery and secreted components for subcomplex formation.

The type VI secretion system (T6SS) is widely distributed in pathogenic Proteobacteria. Sequence and structural analysis of T6SS reveals a resemblance to the T4 bacteriophage tail, in which an outer sheath structure contracts an internal tube for injecting nucleic acid into bacterial cells. However,...

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Autores principales:	Jer-Sheng Lin, Lay-Sun Ma, Erh-Min Lai
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e358c5ff8aaf4e3cac8630dc171eb22e
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spelling	oai:doaj.org-article:e358c5ff8aaf4e3cac8630dc171eb22e2021-11-18T07:38:27ZSystematic dissection of the agrobacterium type VI secretion system reveals machinery and secreted components for subcomplex formation.1932-620310.1371/journal.pone.0067647https://doaj.org/article/e358c5ff8aaf4e3cac8630dc171eb22e2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23861778/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The type VI secretion system (T6SS) is widely distributed in pathogenic Proteobacteria. Sequence and structural analysis of T6SS reveals a resemblance to the T4 bacteriophage tail, in which an outer sheath structure contracts an internal tube for injecting nucleic acid into bacterial cells. However, the molecular details of how this phage tail-like T6SS structure is assembled in vivo and executed for exoprotein or effector secretion remain largely unknown. Here, we used a systematic approach to identify T6SS machinery and secreted components and investigate the interaction among the putative sheath and tube components of Agrobacterium tumefaciens. We showed that 14 T6SS components play essential roles in the secretion of the T6SS hallmark exoprotein Hcp. In addition, we discovered a novel T6SS exoprotein, Atu4347, that is dispensable for Hcp secretion. Interestingly, Atu4347 and the putative tube components, Hcp and VgrG, are mainly localized in the cytoplasm but also detected on the bacterial surface. Atu4342 (TssB) and Atu4341 (TssC41) interact with and stabilize each other, which suggests that they are functional orthologs of the sheath components TssB (VipA) and TssC (VipB), respectively. Importantly, TssB interacts directly with the three exoproteins (Hcp, VgrG, and Atu4347), in which Hcp also interacts directly with VgrG-1 on co-purification from Escherichia coli. Further co-immunoprecipitation and pulldown assays revealed these subcomplex(es) in A. tumefaciens and thereby support T6SS functioning as a contractile phage tail-like structure.Jer-Sheng LinLay-Sun MaErh-Min LaiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 7, p e67647 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jer-Sheng Lin Lay-Sun Ma Erh-Min Lai Systematic dissection of the agrobacterium type VI secretion system reveals machinery and secreted components for subcomplex formation.
description	The type VI secretion system (T6SS) is widely distributed in pathogenic Proteobacteria. Sequence and structural analysis of T6SS reveals a resemblance to the T4 bacteriophage tail, in which an outer sheath structure contracts an internal tube for injecting nucleic acid into bacterial cells. However, the molecular details of how this phage tail-like T6SS structure is assembled in vivo and executed for exoprotein or effector secretion remain largely unknown. Here, we used a systematic approach to identify T6SS machinery and secreted components and investigate the interaction among the putative sheath and tube components of Agrobacterium tumefaciens. We showed that 14 T6SS components play essential roles in the secretion of the T6SS hallmark exoprotein Hcp. In addition, we discovered a novel T6SS exoprotein, Atu4347, that is dispensable for Hcp secretion. Interestingly, Atu4347 and the putative tube components, Hcp and VgrG, are mainly localized in the cytoplasm but also detected on the bacterial surface. Atu4342 (TssB) and Atu4341 (TssC41) interact with and stabilize each other, which suggests that they are functional orthologs of the sheath components TssB (VipA) and TssC (VipB), respectively. Importantly, TssB interacts directly with the three exoproteins (Hcp, VgrG, and Atu4347), in which Hcp also interacts directly with VgrG-1 on co-purification from Escherichia coli. Further co-immunoprecipitation and pulldown assays revealed these subcomplex(es) in A. tumefaciens and thereby support T6SS functioning as a contractile phage tail-like structure.
format	article
author	Jer-Sheng Lin Lay-Sun Ma Erh-Min Lai
author_facet	Jer-Sheng Lin Lay-Sun Ma Erh-Min Lai
author_sort	Jer-Sheng Lin
title	Systematic dissection of the agrobacterium type VI secretion system reveals machinery and secreted components for subcomplex formation.
title_short	Systematic dissection of the agrobacterium type VI secretion system reveals machinery and secreted components for subcomplex formation.
title_full	Systematic dissection of the agrobacterium type VI secretion system reveals machinery and secreted components for subcomplex formation.
title_fullStr	Systematic dissection of the agrobacterium type VI secretion system reveals machinery and secreted components for subcomplex formation.
title_full_unstemmed	Systematic dissection of the agrobacterium type VI secretion system reveals machinery and secreted components for subcomplex formation.
title_sort	systematic dissection of the agrobacterium type vi secretion system reveals machinery and secreted components for subcomplex formation.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/e358c5ff8aaf4e3cac8630dc171eb22e
work_keys_str_mv	AT jershenglin systematicdissectionoftheagrobacteriumtypevisecretionsystemrevealsmachineryandsecretedcomponentsforsubcomplexformation AT laysunma systematicdissectionoftheagrobacteriumtypevisecretionsystemrevealsmachineryandsecretedcomponentsforsubcomplexformation AT erhminlai systematicdissectionoftheagrobacteriumtypevisecretionsystemrevealsmachineryandsecretedcomponentsforsubcomplexformation
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Systematic dissection of the agrobacterium type VI secretion system reveals machinery and secreted components for subcomplex formation.

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