Glycine residues in the hydrophobic core of the GspB signal sequence route export toward the accessory Sec pathway.

ABSTRACT: The Streptococcus gordonii cell surface glycoprotein GspB mediates high-affinity binding to distinct sialylated carbohydrate structures on human platelets and salivary proteins. GspB is glycosylated in the cytoplasm of S. gordonii and is then transported to the cell surface via a dedicated transport system that includes the accessory Sec components SecA2 and SecY2. The means by which the GspB preprotein is selectively recognized by the accessory Sec system have not been characterized fully. GspB has a 90-residue amino-terminal signal sequence that displays a traditional tripartite structure, with an atypically long amino-terminal (N) region followed by hydrophobic (H) and cleavage regions. In this report, we investigate the relative importance of the N and H regions of the GspB signal pept

SUBMITTER: Bensing BA 

PROVIDER: S-EPMC1913339 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature