Bacterial tyrosine kinases: evolution, biological function and structural insights

Christophe Grangeasse, Sylvie Nessler, Ivan Mijakovic

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Reversible protein phosphorylation is a major mechanism in the regulation of fundamental signalling events in all living organisms. Bacteria have been shown to possess a versatile repertoire of protein kinases, including histidine and aspartic acid kinases, serine/threonine kinases, and more recently tyrosine and arginine kinases. Tyrosine phosphorylation is today recognized as a key regulatory device of bacterial physiology, linked to exopolysaccharide production, virulence, stress response and DNA metabolism. However, bacteria have evolved tyrosine kinases that share no resemblance with their eukaryotic counterparts and are unique in exploiting the ATP/GTP-binding Walker motif to catalyse autophosphorylation and substrate phosphorylation on tyrosine. These enzymes, named BY-kinases (for Bacterial tYrosine kinases), have been identified in a majority of sequenced bacterial genomes, and to date no orthologues have been found in Eukarya. The aim of this review was to present the most recent knowledge about BY-kinases by focusing primarily on their evolutionary origin, structural and functional aspects, and emerging regulatory potential based on recent bacterial phosphoproteomic studies.
Original languageEnglish
JournalPhilosophical Transactions of the Royal Society B: Biological Sciences
Issue number1602
Pages (from-to)2640-2655
Publication statusPublished - 2012
Externally publishedYes


  • evolution
  • genome
  • stress response
  • Microorganisms (Bacteria, Eubacteria, Microorganisms) - Bacteria [05000] bacteria common
  • arginine kinase 9026-70-4 EC
  • aspartic acid kinase
  • ATP 111839-44-2
  • DNA metabolism
  • exopolysaccharide
  • GTP 86-01-1
  • histidine 4998-57-6
  • serine/threonine kinase EC
  • tyrosine 556-03-6
  • tyrosine kinase 80449-02-1
  • 01500, Evolution
  • 10062, Biochemistry studies - Nucleic acids, purines and pyrimidines
  • 10064, Biochemistry studies - Proteins, peptides and amino acids
  • 10802, Enzymes - General and comparative studies: coenzymes
  • 31000, Physiology and biochemistry of bacteria
  • Biochemistry and Molecular Biophysics
  • Enzymology
  • Evolution and Adaptation

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