YopD self-assembly and binding to LcrV facilitate type III secretion activity by Yersinia pseudotuberculosisShow others and affiliations
2010 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 285, no 33, p. 25269-25284Article in journal (Refereed) Published
Abstract [en]
YopD-like translocator proteins encoded by several Gram-negative bacteria are important for type III secretion-dependent delivery of anti-host effectors into eukaryotic cells. This probably depends on their ability to form pores in the infected cell plasma membrane, through which effectors may gain access to the cell interior. In addition, Yersinia YopD is a negative regulator essential for the control of effector synthesis and secretion. As a prerequisite for this functional duality, YopD may need to establish molecular interactions with other key T3S components. A putative coiled-coil domain and an alpha-helical amphipathic domain, both situated in the YopD C terminus, may represent key protein-protein interaction domains. Therefore, residues within the YopD C terminus were systematically mutagenized. All 68 mutant bacteria were first screened in a variety of assays designed to identify individual residues essential for YopD function, possibly by providing the interaction interface for the docking of other T3S proteins. Mirroring the effect of a full-length yopD gene deletion, five mutant bacteria were defective for both yop regulatory control and effector delivery. Interestingly, all mutations clustered to hydrophobic amino acids of the amphipathic domain. Also situated within this domain, two additional mutants rendered YopD primarily defective in the control of Yop synthesis and secretion. Significantly, protein-protein interaction studies revealed that functionally compromised YopD variants were also defective in self-oligomerization and in the ability to engage another translocator protein, LcrV. Thus, the YopD amphipathic domain facilitates the formation of YopD/YopD and YopD/LcrV interactions, two critical events in the type III secretion process.
Place, publisher, year, edition, pages
American Society for Biochemistry and Molecular Biology , 2010. Vol. 285, no 33, p. 25269-25284
Keywords [en]
Bacteria, Bacterial Genetics, Protein Cross-linking, Protein-Protein Interactions, Secretion, Yersinia, Amphipathic, Coiled-coil, Pore Formation, Regulation
National Category
Microbiology in the medical area
Research subject
Infectious Diseases
Identifiers
URN: urn:nbn:se:umu:diva-41848DOI: 10.1074/jbc.M110.144311ISI: 000280682400020PubMedID: 20525687Scopus ID: 2-s2.0-77955495219OAI: oai:DiVA.org:umu-41848DiVA, id: diva2:407950
2011-04-112011-04-012023-03-24Bibliographically approved
In thesis