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http://purl.uniprot.org/citations/18295742http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18295742http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18295742http://www.w3.org/2000/01/rdf-schema#comment"Porphyromonas gingivalis, a major etiological bacterium of periodontal diseases, produces a unique lysine-specific cysteine proteinase (Lys-gingipain, Kgp) implicated in the virulence of this organism. Our observations show the expression of a catalytically active recombinant Kgp in a P. gingivalis Kgp-null mutant and the restoration of its functions by the use of a shuttle plasmid vector stable in P. gingivalis. The Kgp-expressing mutant exhibited a similar catalytic activity to that of the wild-type strain. This mutant also restored the ability to form black-pigmented colonies on blood agar plates and to generate a 19-kDa haemoglobin receptor protein responsible for haemoglobin binding. In order to establish the importance of the active-site Cys residue and elucidate its role in bacterial black pigmentation we constructed three Kgp mutants with changed potential active-site Cys residues. The cells expressing a single mutation (C476A) showed the high Kgp activity and the black pigmentation. In contrast, the cells expressing the single mutant (C477A) and the double mutant (C476A/C477A) exhibited neither Kgp activity nor black pigmentation. These results indicate that the 477th Cys residue is essential for both the Kgp activity and the black pigmentation of P. gingivalis."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.org/dc/terms/identifier"doi:10.1016/j.archoralbio.2008.01.004"xsd:string
http://purl.uniprot.org/citations/18295742http://purl.org/dc/terms/identifier"doi:10.1016/j.archoralbio.2008.01.004"xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Kato Y."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Kato Y."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Ishida Y."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Ishida Y."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Hu J."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Hu J."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Nakayama K."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Nakayama K."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Okamoto K."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Okamoto K."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Yamamoto K."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Yamamoto K."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Kadowaki T."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Kadowaki T."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Sakai E."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Sakai E."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Tsukuba T."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/author"Tsukuba T."xsd:string
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18295742http://purl.uniprot.org/core/date"2008"xsd:gYear