ArticleFrontiers in cellular and infection microbiology2013
The SycN/YscB chaperone-binding domain of YopN is required for the calcium-dependent regulation of Yop secretion by Yersinia pestis.
Article in Frontiers in cellular and infection microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Class II chaperones: indispensable components of the Gram-negative bacterial T3SS as guardians of translocators.Archives of microbiology · 2026Review
- Gene Regulatory Network of the Noncoding RNAMicroorganisms · 2022Article
- The gatekeeper of Yersinia type III secretion is under RNA thermometer control.PLoS pathogens · 2021Article
- Context-Dependent Action of Scc4 Reinforces Control of the Type III Secretion System.Journal of bacteriology · 2020Article
- Prophage-Related GeneFrontiers in cellular and infection microbiology · 2020Article
- Identification of specific sequence motif of YopN of Yersinia pseudotuberculosis required for systemic infection.Virulence · 2019Article
- Disruption of the NlpD lipoprotein of the plague pathogen Yersinia pestis affects iron acquisition and the activity of the twin-arginine translocation system.PLoS neglected tropical diseases · 2019Article
- YopN Is Required for Efficient Effector Translocation and Virulence in Yersinia pseudotuberculosis.Infection and immunity · 2018Article
- Steps for Shigella Gatekeeper Protein MxiC Function in Hierarchical Type III Secretion Regulation.The Journal of biological chemistry · 2017Article
- Article
- YopN and TyeA Hydrophobic Contacts Required for Regulating Ysc-Yop Type III Secretion Activity by Yersinia pseudotuberculosis.Frontiers in cellular and infection microbiology · 2016Article
- Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae.The Journal of biological chemistry · 2014Article
- The pathogenic Yersiniae--advances in the understanding of physiology and virulence.Frontiers in cellular and infection microbiology · 2013Article
- Genetically engineered frameshifted YopN-TyeA chimeras influence type III secretion system function in Yersinia pseudotuberculosis.PloS one · 2013Article
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Abstract
Numerous Gram-negative bacterial pathogens employ type III secretion systems (T3SSs) to inject effector proteins into eukaryotic cells. The activation of the type III secretion (T3S) process is tightly controlled in all T3SSs. In Yersinia pestis, the secretion of effector proteins, termed Yersinia outer proteins (Yops), is regulated by the activity of the YopN/SycN/YscB/TyeA complex. YopN is a secreted protein that interacts with the SycN/YscB chaperone via an N-terminal chaperone-binding domain (CBD) and with TyeA via a C-terminal TyeA-binding domain (TBD). Efficient YopN secretion is dependent upon its N-terminal secretion signal (SS), CBD, and the SycN/YscB chaperone. In this study, we investigate the role of the YopN CBD in the regulation of Yop secretion. Analysis of YopE/YopN hybrid proteins in which the YopN SS or SS and CBD were replaced with the analogous regions of YopE indicated that the YopN CBD or SycN/YscB chaperone play a role in the regulation of Yop secretion that is independent of their established roles in YopN secretion. To further analyze the role of the YopN CBD in the regulation of Yop secretion a series of tetra-alanine substitution mutants were generated throughout the YopN CBD. A number of these mutants exhibited a defect in the regulation of Yop secretion but showed no defect in YopN secretion or in the interaction of YopN with the SycN/YscB chaperone. Finally, conditions were established that enabled YopN and TyeA to regulate Yop secretion in the absence of the SycN/YscB chaperone. Importantly, a number of the YopN CBD mutants maintained their defect in the regulation of Yop secretion even under the established SycN/YscB chaperone-independent conditions. These studies establish a role for the CBD region of YopN in the regulation of Yop secretion that is independent from its role in YopN secretion or in the binding of the SycN/YscB chaperone.
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