Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology

• Published in: Trends in biochemical sciences (Amsterdam. Regular ed.) Vol. 32; no. 2; pp. 86 - 94
• Main Authors: Grangeasse, Christophe, Cozzone, Alain J., Deutscher, Josef, Mijakovic, Ivan
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.02.2007; Elsevier
• Subjects: Amino Acid Sequence; Bacteria; Bacterial Physiological Phenomena; Bacterial Physiology; Bacterial Proteins; Bacterial Proteins - metabolism; Biochemistry, Molecular Biology; Life Sciences; Molecular biology; Molecular Sequence Data; Phosphorylation; Protein Processing, Post-Translational; Protein-Tyrosine Kinases; Protein-Tyrosine Kinases - metabolism; Sequence Homology, Amino Acid; Tyrosine; Tyrosine - metabolism; BACTERIA; PHOSPHORYLLATION; BY-KINASE; GENE EXPRESSION REGULATION; TYROSINE KINASE; BACTERIAL PROTEIN; PHOSPHOTRANSFERASE SYSTEM; PTS
• ISSN: 0968-0004; 1362-4326
• DOI: 10.1016/j.tibs.2006.12.004

Tyrosine phosphorylation is a key device in numerous cellular functions in eukaryotes, but in bacteria this protein modification was largely ignored until the mid-1990s. The first conclusive evidence of bacterial tyrosine phosphorylation came only a decade ago. Since then, several tyrosine kinases exhibiting unexpected features have been identified in a variety of bacteria. These enzymes use homologues of Walker motifs of nucleotide-binding proteins for their catalytic mechanism, thus defining an idiosyncratic type of bacterial tyrosine kinases. Recently, bacterial tyrosine kinases have been found to phosphorylate an increasing list of endogenous protein substrates. This discovery contributes to the emerging picture that bacterial tyrosine phosphorylation is an important regulatory arsenal of bacterial physiology in addition to the classical serine/threonine kinases, and the ‘two-component’ and phosphotransferase systems.