Article
Licensed
Unlicensed
Requires Authentication
Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes
-
Maryta Sztukowska
Published/Copyright:
September 1, 2012
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
You are currently not able to access this content.
You are currently not able to access this content.
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: The universe of proteolytic networks and mechanisms
- Highlight: 7th General Meeting of the International Proteolysis Society
- Current and prospective applications of non-proteinogenic amino acids in profiling of proteases substrate specificity
- Understanding the substrate specificity of conventional calpains
- Protease-dependent mechanisms of complement evasion by bacterial pathogens
- An ensemble view of thrombin allostery
- Processive proteolysis by γ-secretase and the mechanism of Alzheimer’s disease
- TMPRSS4 is a type II transmembrane serine protease involved in cancer and viral infections
- A catalogue of putative HIV-1 protease host cell substrates
- Identifi cation of protease exosite-interacting peptides that enhance substrate cleavage kinetics
- A plant Kunitz-type inhibitor mimics bradykinin-induced cytosolic calcium increase and intestinal smooth muscle contraction
- Characterisation and metabolism of astroglia-rich primary cultures from cathepsin K-deficient mice
- Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes
- Review
- Synthesis and biological actions of diphosphoinositol phosphates (inositol pyrophosphates), regulators of cell homeostasis
- Minireviews
- Redox Biology on the rise
- Adipose triglyceride lipase in immune response, inflammation, and atherosclerosis
- Research Articles/Short Communications
- Protein Structure and Function
- Insights into the modulation of optimum pH by a single histidine residue in arginine deiminase from Pseudomonas aeruginosa
Keywords for this article
cysteine protease;
limited proteolysis;
periodontitis;
Porphyromonas gingivalis;
posttranslational processing
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: The universe of proteolytic networks and mechanisms
- Highlight: 7th General Meeting of the International Proteolysis Society
- Current and prospective applications of non-proteinogenic amino acids in profiling of proteases substrate specificity
- Understanding the substrate specificity of conventional calpains
- Protease-dependent mechanisms of complement evasion by bacterial pathogens
- An ensemble view of thrombin allostery
- Processive proteolysis by γ-secretase and the mechanism of Alzheimer’s disease
- TMPRSS4 is a type II transmembrane serine protease involved in cancer and viral infections
- A catalogue of putative HIV-1 protease host cell substrates
- Identifi cation of protease exosite-interacting peptides that enhance substrate cleavage kinetics
- A plant Kunitz-type inhibitor mimics bradykinin-induced cytosolic calcium increase and intestinal smooth muscle contraction
- Characterisation and metabolism of astroglia-rich primary cultures from cathepsin K-deficient mice
- Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes
- Review
- Synthesis and biological actions of diphosphoinositol phosphates (inositol pyrophosphates), regulators of cell homeostasis
- Minireviews
- Redox Biology on the rise
- Adipose triglyceride lipase in immune response, inflammation, and atherosclerosis
- Research Articles/Short Communications
- Protein Structure and Function
- Insights into the modulation of optimum pH by a single histidine residue in arginine deiminase from Pseudomonas aeruginosa
