title: Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes.
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.
authors.affiliation: Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, Louisville, KY 40202, USA.
authors.forename: Maryta
authors.initials: M
authors.lastname: Sztukowska
authors.forename: Florian
authors.initials: F
authors.lastname: Veillard
authors.forename: Barbara
authors.initials: B
authors.lastname: Potempa
authors.forename: Matthew
authors.initials: M
authors.lastname: Bogyo
authors.forename: Jan J
authors.initials: JJ
authors.lastname: Enghild
authors.forename: Ida B
authors.initials: IB
authors.lastname: Thogersen
authors.forename: Ky-Anh
authors.initials: KA
authors.lastname: Nguyen
authors.forename: Jan
authors.initials: J
authors.lastname: Potempa
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D001483:Base Sequence; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000080867:Gingipain Cysteine Endopeptidases; D008969:Molecular Sequence Data
chemical_list: D018829:Adhesins, Bacterial; D000080867:Gingipain Cysteine Endopeptidases; D003546:Cysteine Endopeptidases