ArticleFrontiers in cellular and infection microbiology2016
YopN and TyeA Hydrophobic Contacts Required for Regulating Ysc-Yop Type III Secretion Activity by Yersinia pseudotuberculosis.
Article in Frontiers in cellular and infection microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed.
- Fis suppresses late-stage virulence gene expression in Yersinia pseudotuberculosis at environmental temperatures.PLoS pathogens · 2026Article
- Recognition of a translocation motif in the regulator HpaA fromFrontiers in plant science · 2022Article
- The gatekeeper of Yersinia type III secretion is under RNA thermometer control.PLoS pathogens · 2021Article
- A T3SS Regulator Mutant ofFrontiers in cellular and infection microbiology · 2020Article
- Identification of specific sequence motif of YopN of Yersinia pseudotuberculosis required for systemic infection.Virulence · 2019Article
- YopN Is Required for Efficient Effector Translocation and Virulence in Yersinia pseudotuberculosis.Infection and immunity · 2018Article
- Heterologous Complementation Studies With the YscX and YscY Protein Families Reveals a Specificity forFrontiers in cellular and infection microbiology · 2018Article
- Hierarchical protein targeting and secretion is controlled by an affinity switch in the type III secretion system of enteropathogenicThe EMBO journal · 2017Article
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7 authors.
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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.
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