Separation of novel phosphoproteins of Porphyromonas gingivalis using phosphate‐affinity chromatography |
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| Authors: | Masashi Izumigawa Yoshiaki Hasegawa Ryota Ikai Toshi Horie Megumi Inomata Takeshi Into Noriyuki Kitai Fuminobu Yoshimura Yukitaka Murakami |
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| Institution: | 1. Department of Oral Microbiology, Asahi University School of Dentistry, 1851‐1 Hozumi, Mizuho, Gifu 501‐0296, Japan;2. Department of Microbiology, School of Dentistry, Aichi Gakuin University, 1‐100 Kusumoto‐cho, Chikusa‐ku, Nagoya 464‐8650, Aichi, Japan;3. Department of Community Oral Health, Asahi University School of Dentistry, 1851‐1 Hozumi, Mizuho, Gifu 501‐0296, Japan;4. Department of Orthodontic, Asahi University School of Dentistry, 1851‐1 Hozumi, Mizuho, Gifu 501‐0296, Japan |
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| Abstract: | Phosphorylation of serine, threonine and tyrosine is a central mechanism for regulating the structure and function of proteins in both eukaryotes and prokaryotes. However, the action of phosphorylated proteins present in Porphyromonas gingivalis, a major periodontopathogen, is not fully understood. Here, six novel phosphoproteins that possess metabolic activities were identified, namely PGN_0004, PGN_0375, PGN_0500, PGN_0724, PGN_0733 and PGN_0880, having been separated by phosphate‐affinity chromatography. The identified proteins were detectable by immunoblotting specific to phosphorylated Ser (P‐Ser), P‐Thr, and/or P‐Tyr. These results imply that novel phosphorylated proteins might play an important role for regulation of metabolism in P. gingivalis. |
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| Keywords: | periodontal disease phosphate‐affinity chromatography phosphoprotein Porphyromonas gingivalis |
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