Characterization of the secretion pathway of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans.

ABSTRACT: The extracellular matrix protein adhesin A (EmaA) surface antennae-like structures of the periodontal pathogen Aggregatibacter actinomycetemcomitans are composed of three identical protein monomers. Recently, we have demonstrated that the protein is synthesized with an extended signal peptide of 56 amino acids necessary for membrane targeting and protein translocation. In this study, EmaA secretion was demonstrated to be reliant on a chaperone-dependent secretion pathway. Deletion of secB partially reduced but did not abolish the amount of EmaA in the membrane. This observation was attributed to an increase in the synthesis of DnaK in the ΔsecB strain. Overexpression of a DnaK substitution mutant (A174T), with diminished activity, in the ΔsecB strain further reduced the amount of EmaA in t

SUBMITTER: Jiang X 

PROVIDER: S-EPMC3442948 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature