YopN and TyeA Hydrophobic Contacts Required for Regulating Ysc-Yop Type III Secretion Activity by Yersinia pseudotuberculosis.

2.50
Hdl Handle:
http://hdl.handle.net/10033/621139
Title:
YopN and TyeA Hydrophobic Contacts Required for Regulating Ysc-Yop Type III Secretion Activity by Yersinia pseudotuberculosis.
Authors:
Amer, Ayad A A; Gurung, Jyoti M; Costa, Tiago R D; Ruuth, Kristina; Zavialov, Anton V ( 0000-0001-6191-5931 ) ; Forsberg, Åke; Francis, Matthew S
Abstract:
Yersinia bacteria target Yop effector toxins to the interior of host immune cells by the Ysc-Yop type III secretion system. A YopN-TyeA heterodimer is central to controlling Ysc-Yop targeting activity. A + 1 frameshift event in the 3-prime end of yopN can also produce a singular secreted YopN-TyeA polypeptide that retains some regulatory function even though the C-terminal coding sequence of this YopN differs greatly from wild type. Thus, this YopN C-terminal segment was analyzed for its role in type III secretion control. Bacteria producing YopN truncated after residue 278, or with altered sequence between residues 279 and 287, had lost type III secretion control and function. In contrast, YopN variants with manipulated sequence beyond residue 287 maintained full control and function. Scrutiny of the YopN-TyeA complex structure revealed that residue W279 functioned as a likely hydrophobic contact site with TyeA. Indeed, a YopN W279G mutant lost all ability to bind TyeA. The TyeA residue F8 was also critical for reciprocal YopN binding. Thus, we conclude that specific hydrophobic contacts between opposing YopN and TyeA termini establishes a complex needed for regulating Ysc-Yop activity.
Affiliation:
Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7, 38124 Braunschweig, Germany.
Citation:
YopN and TyeA Hydrophobic Contacts Required for Regulating Ysc-Yop Type III Secretion Activity by Yersinia pseudotuberculosis. 2016, 6:66 Front Cell Infect Microbiol
Journal:
Frontiers in cellular and infection microbiology
Issue Date:
2016
URI:
http://hdl.handle.net/10033/621139
DOI:
10.3389/fcimb.2016.00066
PubMed ID:
27446813
Type:
Article
Language:
en
ISSN:
2235-2988
Appears in Collections:
publications of the junior research group infection biology of Salmonella (IBIS)

Full metadata record

DC FieldValue Language
dc.contributor.authorAmer, Ayad A Aen
dc.contributor.authorGurung, Jyoti Men
dc.contributor.authorCosta, Tiago R Den
dc.contributor.authorRuuth, Kristinaen
dc.contributor.authorZavialov, Anton Ven
dc.contributor.authorForsberg, Åkeen
dc.contributor.authorFrancis, Matthew Sen
dc.date.accessioned2017-10-17T09:50:39Z-
dc.date.available2017-10-17T09:50:39Z-
dc.date.issued2016-
dc.identifier.citationYopN and TyeA Hydrophobic Contacts Required for Regulating Ysc-Yop Type III Secretion Activity by Yersinia pseudotuberculosis. 2016, 6:66 Front Cell Infect Microbiolen
dc.identifier.issn2235-2988-
dc.identifier.pmid27446813-
dc.identifier.doi10.3389/fcimb.2016.00066-
dc.identifier.urihttp://hdl.handle.net/10033/621139-
dc.description.abstractYersinia bacteria target Yop effector toxins to the interior of host immune cells by the Ysc-Yop type III secretion system. A YopN-TyeA heterodimer is central to controlling Ysc-Yop targeting activity. A + 1 frameshift event in the 3-prime end of yopN can also produce a singular secreted YopN-TyeA polypeptide that retains some regulatory function even though the C-terminal coding sequence of this YopN differs greatly from wild type. Thus, this YopN C-terminal segment was analyzed for its role in type III secretion control. Bacteria producing YopN truncated after residue 278, or with altered sequence between residues 279 and 287, had lost type III secretion control and function. In contrast, YopN variants with manipulated sequence beyond residue 287 maintained full control and function. Scrutiny of the YopN-TyeA complex structure revealed that residue W279 functioned as a likely hydrophobic contact site with TyeA. Indeed, a YopN W279G mutant lost all ability to bind TyeA. The TyeA residue F8 was also critical for reciprocal YopN binding. Thus, we conclude that specific hydrophobic contacts between opposing YopN and TyeA termini establishes a complex needed for regulating Ysc-Yop activity.en
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAnimalsen
dc.subject.meshBacterial Outer Membrane Proteinsen
dc.subject.meshBacterial Proteinsen
dc.subject.meshBiological Transporten
dc.subject.meshCalciumen
dc.subject.meshCarrier Proteinsen
dc.subject.meshCell Lineen
dc.subject.meshDNA, Bacterialen
dc.subject.meshGene Expression Regulation, Bacterialen
dc.subject.meshGenes, Bacterialen
dc.subject.meshHydrophobic and Hydrophilic Interactionsen
dc.subject.meshMacrophagesen
dc.subject.meshMembrane Proteinsen
dc.subject.meshMiceen
dc.subject.meshModels, Molecularen
dc.subject.meshMutagenesis, Site-Directeden
dc.subject.meshProtein Interaction Domains and Motifsen
dc.subject.meshProtein Stabilityen
dc.subject.meshProtein Translocation Systemsen
dc.subject.meshSequence Analysisen
dc.subject.meshSequence Deletionen
dc.subject.meshTemperatureen
dc.subject.meshTwo-Hybrid System Techniquesen
dc.subject.meshType III Secretion Systemsen
dc.subject.meshYersinia pseudotuberculosisen
dc.titleYopN and TyeA Hydrophobic Contacts Required for Regulating Ysc-Yop Type III Secretion Activity by Yersinia pseudotuberculosis.en
dc.typeArticleen
dc.contributor.departmentHelmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7, 38124 Braunschweig, Germany.en
dc.identifier.journalFrontiers in cellular and infection microbiologyen
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