YopD self-assembly and binding to LcrV facilitate type III secretion activity by Yersinia pseudotuberculosis.

ABSTRACT: 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 systematicall

SUBMITTER: Costa TR 

PROVIDER: S-EPMC2919090 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature