Separation of novel phosphoproteins of Porphyromonas gingivalis using phosphate‐affinity chromatography. (October 2016)

• Record Type: Journal Article
• Authors: Izumigawa, Masashi; Hasegawa, Yoshiaki; Ikai, Ryota; Horie, Toshi; Inomata, Megumi; Into, Takeshi; Kitai, Noriyuki; Yoshimura, Fuminobu; Murakami, Yukitaka
• Is Part Of: Microbiology and immunology. Volume 60:Number 10(2016:Oct.)
• Page Start: 702
• Page End: 707
• Publication Date: 2016-10
• Subjects: periodontal disease -- phosphate‐affinity chromatography -- phosphoprotein -- Porphyromonas gingivalis; Microbiology -- Periodicals; Immunology -- Periodicals; Allergy and Immunology -- Periodicals; Microbiology -- Periodicals; Microbiologie -- Périodiques; Immunologie -- Périodiques; 579
• DOI: 10.1111/1348-0421.12441
• Languages: English
• ISSNs: 0385-5600

Abstract

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 .