Format

Send to

Choose Destination
Biol Chem. 2012 Sep;393(9):971-7. doi: 10.1515/hsz-2012-0175.

Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes.

Author information

1
Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, Louisville, KY 40202, USA.

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.

PMID:
22944696
PMCID:
PMC3488288
DOI:
10.1515/hsz-2012-0175
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Sheridan PubFactory Icon for PubMed Central
Loading ...
Support Center