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Biochem Biophys Res Commun. 1996 Jul 25;224(3):605-10.

Characterization of a Porphyromonas gingivalis gene prtR that encodes an arginine-specific thiol proteinase and multiple adhesins.

Author information

1
Biochemistry and Molecular Biology Unit, School of Dental Science, University of Melbourne, Victoria, Australia.

Abstract

Cysteine proteinases of Porphyromonas gingivalis have been implicated as major virulence factors in the development of periodontitis. Several groups have reported the characterisation of similar genes encoding the same arginine-specific thiol proteinase from P. gingivalis; however, the reported size and structure of the genes have varied. We report here the complete nucleotide sequence of the gene prtR that encodes a polyprotein containing the Arg-specific proteinase and multiple haemagglutinins/adhesins. The nascent polyprotein consists of a putative leader sequence and a prosequence followed by the 45 kDa Arg-specific proteinase and 44, 15, 17 and 27 kDa sequence-related adhesins in that order. The size and structure of the prtR are consistent with the size of the mRNA transcript (5.3 kb) and the size and sequences of the individual protein components purified from P. gingivalis.

PMID:
8713096
DOI:
10.1006/bbrc.1996.1073
[Indexed for MEDLINE]

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