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FEMS Microbiol Rev. 2016 Sep;40(5):625-47. doi: 10.1093/femsre/fuw020. Epub 2016 Jul 29.

Protein phosphorylation and its role in archaeal signal transduction.

Author information

1
Molecular Enzyme Technology and Biochemistry, Biofilm Centre, Faculty of Chemistry, University of Duisburg-Essen, Universitätsstraße 5, 45141 Essen, Germany.
2
Molecular Biology of Archaea, Institute of Biology II, University of Freiburg, Schänzlestrasse 1, 79104 Freiburg, Germany.
3
ChELSI Institute, Department of Chemical and Biological Engineering, The University of Sheffield, Mappin Street, Sheffield S1 3JD, UK.
4
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.
5
Molecular Enzyme Technology and Biochemistry, Biofilm Centre, Faculty of Chemistry, University of Duisburg-Essen, Universitätsstraße 5, 45141 Essen, Germany bettina.siebers@uni-due.de.

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.

KEYWORDS:

Archaea; Crenarchaeota; Euryarchaeota; protein kinase; protein phosphatase; regulation; reversible protein phosphorylation; signal transduction

PMID:
27476079
PMCID:
PMC5007285
DOI:
10.1093/femsre/fuw020
[Indexed for MEDLINE]
Free PMC Article

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