title: Protein phosphorylation and its role in archaeal signal transduction.
abstract: Reversible protein phosphorylation is the main mechanism of signal transduction that enables cells to rapidly respond to environmental changes by controlling the functional properties of proteins in response to external stimuli. However, whereas signal transduction is well studied in Eukaryotes and Bacteria, the knowledge in Archaea is still rather scarce. Archaea are special with regard to protein phosphorylation, due to the fact that the two best studied phyla, the Euryarchaeota and Crenarchaeaota, seem to exhibit fundamental differences in regulatory systems. Euryarchaeota (e.g. halophiles, methanogens, thermophiles), like Bacteria and Eukaryotes, rely on bacterial-type two-component signal transduction systems (phosphorylation on His and Asp), as well as on the protein phosphorylation on Ser, Thr and Tyr by Hanks-type protein kinases. Instead, Crenarchaeota (e.g. acidophiles and (hyper)thermophiles) only depend on Hanks-type protein phosphorylation. In this review, the current knowledge of reversible protein phosphorylation in Archaea is presented. It combines results from identified phosphoproteins, biochemical characterization of protein kinases and protein phosphatases as well as target enzymes and first insights into archaeal signal transduction by biochemical, genetic and polyomic studies.
authors.affiliation: Molecular Enzyme Technology and Biochemistry, Biofilm Centre, Faculty of Chemistry, University of Duisburg-Essen, Universitätsstraße 5, 45141 Essen, Germany.
authors.forename: Dominik
authors.initials: D
authors.lastname: Esser
authors.affiliation: Molecular Biology of Archaea, Institute of Biology II, University of Freiburg, Schänzlestrasse 1, 79104 Freiburg, Germany.
authors.forename: Lena
authors.initials: L
authors.lastname: Hoffmann
authors.affiliation: ChELSI Institute, Department of Chemical and Biological Engineering, The University of Sheffield, Mappin Street, Sheffield S1 3JD, UK.
authors.forename: Trong Khoa
authors.initials: TK
authors.lastname: Pham
authors.affiliation: Molecular Enzyme Technology and Biochemistry, Biofilm Centre, Faculty of Chemistry, University of Duisburg-Essen, Universitätsstraße 5, 45141 Essen, Germany.
authors.forename: Christopher
authors.initials: C
authors.lastname: Bräsen
authors.affiliation: ChELSI Institute, Department of Chemical and Biological Engineering, The University of Sheffield, Mappin Street, Sheffield S1 3JD, UK.
authors.forename: Wen
authors.initials: W
authors.lastname: Qiu
authors.affiliation: ChELSI Institute, Department of Chemical and Biological Engineering, The University of Sheffield, Mappin Street, Sheffield S1 3JD, UK School of Chemical Engineering and Advanced Materials, Faculty of Science, Agriculture and Engineering, Newcastle University, Newcastle upon Tyne NE1 7RU, UK.
authors.forename: Phillip C
authors.initials: PC
authors.lastname: Wright
authors.affiliation: Molecular Biology of Archaea, Institute of Biology II, University of Freiburg, Schänzlestrasse 1, 79104 Freiburg, Germany.
authors.forename: Sonja-Verena
authors.initials: SV
authors.lastname: Albers
authors.affiliation: Molecular Enzyme Technology and Biochemistry, Biofilm Centre, Faculty of Chemistry, University of Duisburg-Essen, Universitätsstraße 5, 45141 Essen, Germany bettina.siebers@uni-due.de.
authors.forename: Bettina
authors.initials: B
authors.lastname: Siebers
mesh_terms: D019843:Archaeal Proteins / Q000378:metabolism*; D019615:Crenarchaeota / Q000235:genetics / Q000378:metabolism*; D019605:Euryarchaeota / Q000235:genetics / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010766:Phosphorylation / Q000235:genetics*; D000072417:Protein Domains / Q000235:genetics; D011494:Protein Kinases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000235:genetics / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology
chemical_list: D019843:Archaeal Proteins; D011494:Protein Kinases; D010749:Phosphoprotein Phosphatases
keywords: Archaea; Crenarchaeota; Euryarchaeota; protein kinase; protein phosphatase; regulation; reversible protein phosphorylation; signal transduction