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Abstract
RgpA and Kgp gingipains are non-covalent complexes of endoprotease catalytic and hemagglutinin-adhesin domains on the surface of Porphyromonas gingivalis. A motif conserved in each domain has been suggested to function as an oligomerization motif. We tested this hypothesis by mutating motif residues to hexahistidine or insertion of hexahistidine tag to disrupt the motif within the Kgp catalytic domain. All modifications led to the secretion of entire Kgp activity into the growth media, predominantly in a form without functional His-tag. This confirmed the role of the conserved motif in correct posttranslational proteolytic processing and assembly of the multidomain complexes.
Keywords: cysteine protease; limited proteolysis; periodontitis; Porphyromonas gingivalis; posttranslational processing
Received: 2012-4-10
Accepted: 2012-5-6
Published Online: 2012-09-01
Published in Print: 2012-09-01
©2012 by Walter de Gruyter Berlin Boston
