title: Exploring the diversity of protein modifications: special bacterial phosphorylation systems.
abstract: Protein modifications not only affect protein homeostasis but can also establish new cellular protein functions and are important components of complex cellular signal sensing and transduction networks. Among these post-translational modifications, protein phosphorylation represents the one that has been most thoroughly investigated. Unlike in eukarya, a large diversity of enzyme families has been shown to phosphorylate and dephosphorylate proteins on various amino acids with different chemical properties in bacteria. In this review, after a brief overview of the known bacterial phosphorylation systems, we focus on more recently discovered and less widely known kinases and phosphatases. Namely, we describe in detail tyrosine- and arginine-phosphorylation together with some examples of unusual serine-phosphorylation systems and discuss their potential role and function in bacterial physiology, and regulatory networks. Investigating these unusual bacterial kinase and phosphatases is not only important to understand their role in bacterial physiology but will help to generally understand the full potential and evolution of protein phosphorylation for signal transduction, protein modification and homeostasis in all cellular life.
authors.affiliation: Systems and Synthetic Biology Division, Department of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg 41296, Sweden Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, 2970 Hørsholm, Denmark.
authors.forename: Ivan
authors.initials: I
authors.lastname: Mijakovic
authors.affiliation: Unité Microbiologie Moléculaire et Biochimie Structurale, UMR 5086-CNRS/ Université Lyon 1, Lyon 69367, France.
authors.forename: Christophe
authors.initials: C
authors.lastname: Grangeasse
authors.affiliation: Institut für Mikrobiologie, Leibniz Universität Hannover, D-30419 Hannover, Germany turgay@ifmb.uni-hannover.de.
authors.forename: Kürşad
authors.initials: K
authors.lastname: Turgay
mesh_terms: D001419:Bacteria / Q000201:enzymology*; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction / Q000502:physiology
chemical_list: D001426:Bacterial Proteins; D010770:Phosphotransferases; D010744:Phosphoric Monoester Hydrolases
keywords: protein arginine phosphorylation; protein homeostasis; protein kinase/phosphatase; protein modification; protein serine/threonine phosphorylation; protein-tyrosine phosphorylation