serthrtyr protein phosphorylation in the archaeon halobacterium salinarum—a representative of the third domain of lifeserthrtyr蛋白质磷酸化的archaeon halobacterium salinarum-a代表第三域的生活.pdfVIP

Ser/Thr/Tyr Protein Phosphorylation in the Archaeon Halobacterium salinarum—A Representative of the Third Domain of Life 1.¤a 2.¤b 2 1¤c 2 Michalis Aivaliotis *, Boris Macek , Florian Gnad , Peter Reichelt , Matthias Mann , Dieter Oesterhelt1 1 Department of Membrane Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany, 2 Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany Abstract 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/ conserv