Most strains of Escherichia coli are motile by multiple, peritrichous flagella, and the motility is regulated by three gene classes, Class I, II and III. In previous studies, the General Secretory Pathway (GSP) protein, GspE, involved in Type II secretion system, interacted with F1iM, a flagella motor protein in E. coli, in the yeast two-hybrid system for detecting protein-protein interaction. FliM is required for assembly of flagella, which (excluding the P and L rings) are assembled via a dedicated type III secretion system. The role of the General Secretory Pathway (type II secretion) in E. coli motility is not known. Interestingly, GspE is one of three homologous proteins (GspE, YggR, HofB) encoded by the E. coli chromosomal genome. We have set out to study the significance of the interaction upon the export and assembly of flagellum structural proteins. Although GspE is not essential for motility, we identified a GspE-dependent motility phenotype. Thus, since both F1iM and GspE affect motility, this supports but does not prove the idea that the previously identified F1iM and GspE interaction plays a role in bacterial motility. In this study, we describe the GspE-dependence of intracellular levels of several E. coli proteins, suggesting a model for how the General Secretory Pathway controls bacterial motility.
|School:||California State University, Long Beach|
|School Location:||United States -- California|
|Source:||MAI 49/01M, Masters Abstracts International|
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