The translocation domain in trimeric autotransporter adhesins is necessary and sufficient for trimerization and autotransportation.

ABSTRACT: Trimeric autotransporter adhesins (TAAs) comprise one of the secretion pathways of the type V secretion system. The mechanism of their translocation across the outer membrane remains unclear, but it most probably occurs by the formation of a hairpin inside the β-barrel translocation unit, leading to transportation of the passenger domain from the C terminus to the N terminus through the lumen of the β-barrel. We further investigated the phenomenon of autotransportation and the rules that govern it. We showed by coexpressing different Escherichia coli immunoglobulin-binding (Eib) proteins that highly similar TAAs could form stochastically mixed structures (heterotrimers). We further investigated this phenomenon by coexpressing two more distantly related TAAs, EibA and YadA. These, however,

SUBMITTER: Mikula KM 

PROVIDER: S-EPMC3272944 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature