Ser/Thr/Tyr Protein Phosphorylation in the Archaeon Halobacterium salinarum—A Representative of the Third Domain of Life

• Published in: PloS one Vol. 4; no. 3; p. e4777
• Main Authors: Aivaliotis, Michalis, Macek, Boris, Gnad, Florian, Reichelt, Peter, Mann, Matthias, Oesterhelt, Dieter
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 10.03.2009; Public Library of Science (PLoS)
• Subjects: Accuracy; Amino acids; Amino Acids - metabolism; Archaea; Bacteria; Biochemistry; Biochemistry/Chemical Biology of the Cell; Biological Evolution; Biomedical materials; Cell culture; Cell division; Cellular signal transduction; Chemical Biology/Protein Chemistry and Proteomics; Chemistry/Biochemistry; Conservation; Deoxyribonucleic acid; Dephosphorylation; DNA; Eukaryotes; Evolution; Genetics and Genomics/Functional Genomics; Genome, Bacterial; Genomes; Genomics; Halobacterium salinarum - genetics; Halobacterium salinarum - metabolism; Histidine; Kinases; Lactococcus lactis; Microbiology; Molecular biology; Phosphatase; Phosphorylation; Physiological aspects; Post-translation; Post-translational modifications; Prokaryotes; Protein kinase; Proteins; Proteomics; Proteomics - methods; Serine - metabolism; Signal Transduction; Stem cells; Studies; Surgical implants; Threonine - metabolism; Transduction; Translation; Trends; Tyrosine - metabolism; Germany
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0004777

In the quest for the origin and evolution of protein phosphorylation, the major regulatory post-translational modification in eukaryotes, the members of archaea, the "third domain of life", play a protagonistic role. A plethora of studies have demonstrated that archaeal proteins are subject to post-translational modification by covalent phosphorylation, but little is known concerning the identities of the proteins affected, the impact on their functionality, the physiological roles of archaeal protein phosphorylation/dephosphorylation, and the protein kinases/phosphatases involved. These limited studies led to the initial hypothesis that archaea, similarly to other prokaryotes, use mainly histidine/aspartate phosphorylation, in their two-component systems representing a paradigm of prokaryotic signal transduction, while eukaryotes mostly use Ser/Thr/Tyr phosphorylation for creating highly sophisticated regulatory networks. In antithesis to the above hypothesis, several studies showed that Ser/Thr/Tyr phosphorylation is also common in the bacterial cell, and here we present the first genome-wide phosphoproteomic analysis of the model organism of archaea, Halobacterium salinarum, proving the existence/conservation of Ser/Thr/Tyr phosphorylation in the "third domain" of life, allowing a better understanding of the origin and evolution of the so-called "Nature's premier" mechanism for regulating the functional properties of proteins.