Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established

• Published in: Journal of molecular microbiology and biotechnology Vol. 9; no. 3-4; pp. 125 - 131
• Main Authors: Deutscher, Josef, Saier, Jr, Milton H
• Format: Journal Article
• Language: English
• Published: Switzerland S. Karger AG 01.01.2005; Karger
• Subjects: Bacteria; Bacteria - metabolism; Bacterial Proteins - metabolism; Life Sciences; Phosphoprotein Phosphatases - metabolism; Phosphorylation; Protein Kinases - metabolism; BACTERIA; PROTEINE PHOSPHATASE; PROTEIN PHOSPHORYLATION; PROTEIN KINASE
• ISSN: 1464-1801; 1660-2412
• DOI: 10.1159/000089641

The first clearly established example of Ser/Thr/Tyr phosphorylation of a bacterial protein was isocitrate dehydrogenase. In 1979, 25 years after the discovery of protein phosphorylation in eukaryotes, this enzyme was reported to become phosphorylated on a serine residue. In subsequent years, numerous other bacterial proteins phosphorylated on Ser, Thr or Tyr were discovered and the corresponding protein kinases and P-protein phosphatases were identified. These protein modifications regulate all kinds of physiological processes. Ser/Thr/Tyr phosphorylation in bacteria therefore seems to play a similar important role as in eukaryotes. Surprisingly, many bacterial protein kinases do not exhibit any similarity to eukaryotic protein kinases, but rather resemble nucleotide-binding proteins or kinases phosphorylating diverse low-molecular-weight substrates.