The Yersinia Enterocolitica Type Three Secretion Chaperone SycO is Integrated into the Yop Regulatory Network and Binds to the Yop Secretion Protein YscM1

Overview

Journal BMC Microbiol

Publisher Biomed Central

Specialty Microbiology

Date 2007 Jul 7

PMID 17612396

Citations 6

Authors

Svea Dittmann

Annika Schmid

Susanna Richter

Konrad Trulzsch

Jurgen Heesemann

Gottfried Wilharm

Affiliations

Soon will be listed here.

Abstract

Background: Pathogenic yersiniae (Y. pestis, Y. pseudotuberculosis, Y. enterocolitica) share a virulence plasmid encoding a type three secretion system (T3SS). This T3SS comprises more than 40 constituents. Among these are the transport substrates called Yops (Yersinia outer proteins), the specific Yop chaperones (Sycs), and the Ysc (Yop secretion) proteins which form the transport machinery. The effectors YopO and YopP are encoded on an operon together with SycO, the chaperone of YopO. The characterization of SycO is the focus of this study.

Results: We have established the large-scale production of recombinant SycO in its outright form. We confirm that Y. enterocolitica SycO forms homodimers which is typical for Syc chaperones. SycO overproduction in Y. enterocolitica decreases secretion of Yops into the culture supernatant suggesting a regulatory role of SycO in type III secretion. We demonstrate that in vitro SycO interacts with YscM1, a negative regulator of Yop expression in Y. enterocolitica. However, the SycO overproduction phenotype was not mediated by YscM1, YscM2, YopO or YopP as revealed by analysis of isogenic deletion mutants.

Conclusion: We present evidence that SycO is integrated into the regulatory network of the Yersinia T3SS. Our picture of the Yersinia T3SS interactome is supplemented by identification of the SycO/YscM1 interaction. Further, our results suggest that at least one additional interaction partner of SycO has to be identified.

Citing Articles

LcrQ Coordinates with the YopD-LcrH Complex To Repress Expression and Control Type III Secretion by Yersinia pseudotuberculosis.

Fei K, Yan H, Zeng X, Huang S, Tang W, Francis M mBio. 2021; 12(3):e0145721.

PMID: 34154409 PMC: 8262909. DOI: 10.1128/mBio.01457-21.

Interrelationship between type three secretion system and metabolism in pathogenic bacteria.

Wilharm G, Heider C Front Cell Infect Microbiol. 2014; 4:150.

PMID: 25386411 PMC: 4209828. DOI: 10.3389/fcimb.2014.00150.

Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.

Buttner D Microbiol Mol Biol Rev. 2012; 76(2):262-310.

PMID: 22688814 PMC: 3372255. DOI: 10.1128/MMBR.05017-11.

Direct and negative regulation of the sycO-ypkA-ypoJ operon by cyclic AMP receptor protein (CRP) in Yersinia pestis.

Zhan L, Yang L, Zhou L, Li Y, Gao H, Guo Z BMC Microbiol. 2009; 9:178.

PMID: 19703315 PMC: 2738681. DOI: 10.1186/1471-2180-9-178.

Cross-talk between type three secretion system and metabolism in Yersinia.

Schmid A, Neumayer W, Trulzsch K, Israel L, Imhof A, Roessle M J Biol Chem. 2009; 284(18):12165-77.

PMID: 19244229 PMC: 2673285. DOI: 10.1074/jbc.M900773200.

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