Role of the alpha-helical linker of the C-terminal translocator in the biogenesis of the serine protease subfamily of autotransporters.

ABSTRACT: Autotransporters are secreted virulence factors that comprise three domains: an N-terminal signal peptide, an internal passenger domain, and a C-terminal beta-domain. The mechanism of passenger translocation across the outer membrane remains undefined, with four models having been proposed: the "hairpin," the "threading," the "multimeric," and the "Omp85 (YaeT)" models. In an attempt to understand autotransporter biogenesis, we screened the sequences of the serine protease subfamily of autotransporters (SPATEs) for conserved features indicative of a common secretion mechanism. Our analyses revealed a strictly conserved 14-amino-acid motif within the predicted alpha-helical linker region, upstream of the beta-domain of SPATEs. We investigated the function of this motif through a mutagenesis

SUBMITTER: Kostakioti M 

PROVIDER: S-EPMC1594850 | biostudies-literature | 2006 Sep

REPOSITORIES: biostudies-literature