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Papers In Press, published online ahead of print January 17, 2003
J. Biol. Chem, 10.1074/jbc.M210564200
Submitted on October 15, 2002
Revised on January 15, 2003
Accepted on January 17, 2003

Sequential autolytic processing activates the zymogen of Arg-gingipain

Jowita Mikolajczyk, Kelly M. Boatright, Henning R. Stennicke, Tamim Nazif, Jan Potempa, Matthew Bogyo, and Guy S. Salvesen

Burnham Institute, La Jolla, CA 92037

Corresponding Author: gsalvesen{at}burnham.org

Most proteases are synthesized as inactive precursors to protect the cell's synthetic machinery and allow timing of activation. The mechanisms used to render latency are varied, but tend to be conserved within protease families. Proteases belonging to the caspase family have a unique mechanism mediated by transitions of two surface loops, and on the basis of conservation of mechanism one would expect this to be preserved by caspase relatives. We have been able to express the full length precursor of the Arg-specific caspase relative from the bacterium Porphyromonas gingivalis, Arg-gingipain-B, and we show that it contains N- and C-terminal extensions that render a low amount of latency, meaning that the zymogen is substantially active. Three sequential autolytic processing steps at the N- and C-terminus are required for full activity and the N-propeptide may serve as an intramolecular chaperone, rather than an inhibitory peptide. Each step in activation requires the previous step, and an affinity probe reveals that incremental activity enhancements are achieved in a stepwise manner.


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