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Infect Immun, April 1998, p. 1594-1600, Vol. 66, No. 4
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Maturation of the Arginine-Specific Proteases of Porphyromonas gingivalis W50 Is Dependent on a Functional prR2 Protease Gene

Joseph Aduse-Opoku, Minnie Rangarajan, Katherine A. Young, and Michael A. Curtis*

MRC Molecular Pathogenesis Group, Department of Oral Microbiology, St. Bartholomew's and the Royal London School of Medicine and Dentistry, Queen Mary and Westfield College, London E1 2AA, United Kingdom

Received 22 July 1997/Returned for modification 19 September 1997/Accepted 7 January 1998

The prpR1 of Porphyromonas gingivalis codes for three distinct enzymes with specificity for arginyl peptide bonds termed RI, RIA, and RIB. These three isoforms comprise the majority of the extracellular, arginine-specific protease activity in P. gingivalis W50. RI is a heterodimer in which the catalytic alpha  chain is noncovalently associated with a second chain involved in adherence phenomena. RIA and RIB are both monomeric species. RIA represents the free alpha  chain, and RIB is a highly posttranslationally modified form of the alpha  chain which is exclusively vesicle or membrane associated and migrates as a diffuse band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In previous studies, insertional inactivation of the prpR1 demonstrated that arginine-specific protease activity can also arise from a closely related second gene, prR2. In the present work, the prR2 was insertionally inactivated in P. gingivalis W50 in order to establish the contribution of this locus to the arginine-specific protease activity of this periodontal bacterium. Loss of prR2 function had several effects on prpR1-derived enzymes. First, the total Arg-X activity was reduced by approximately 50% relative to that of the parent strain. The reduction in total activity was a consequence of decreased concentrations of the monomeric enzymes derived from the prpR1, while the heterodimeric enzyme, RI, was unaffected by this mutation. Second, the chromatographic behavior of both the soluble and vesicle- or membrane-associated monomeric enzymes was radically different from the behavior of RIA and RIB from the parent strain. Finally, the vesicle- or membrane-associated enzyme in the prR2 mutant strain lacked the extensive posttranslational additions which are found on RIB in P. gingivalis W50. These data suggest that the product(s) of the prR2 plays a significant role in the maturation pathway of prpR1-derived enzymes, and this may contribute to the coconservation of these two genes in P. gingivalis.

* Corresponding author. Mailing address: MRC Molecular Pathogenesis Group, Dept. of Oral Microbiology, St. Bartholomew's & the Royal London School of Med. & Dentistry, Queen Mary & Westfield Col., 32 Newark St., London E1 2AA, United Kingdom. Phone: 44 171 377 0444. Fax: 44 171 247 3428. E-mail: M.A.Curtis{at}mds.qmw.ac.uk.




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