Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology.
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.
Grangeasse
Christophe
C
Institute of Biology and Chemistry of Proteins, CNRS, University of Lyon, 7 passage du Vercors, 69367 Lyon, France. c.grangeasse@ibcp.fr
Cozzone
Alain J
AJ
Deutscher
Josef
J
Mijakovic
Ivan
I
D000595:Amino Acid Sequence; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014443:Tyrosine / Q000378:metabolism*
D001426:Bacterial Proteins; D014443:Tyrosine; D011505:Protein-Tyrosine Kinases