Ser/Thr/Tyr protein phosphorylation in the archaeon Halobacterium salinarum--a representative of the third domain of life.
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.
Aivaliotis
Michalis
M
Department of Membrane Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.
Macek
Boris
B
Gnad
Florian
F
Reichelt
Peter
P
Mann
Matthias
M
Oesterhelt
Dieter
D
D000596:Amino Acids / Q000378:metabolism*; D001105:Archaea; D005075:Biological Evolution; D016680:Genome, Bacterial; D019617:Halobacterium salinarum / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D040901:Proteomics / Q000379:methods*; D012694:Serine / Q000378:metabolism; D015398:Signal Transduction; D013912:Threonine / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
D000596:Amino Acids; D013912:Threonine; D014443:Tyrosine; D012694:Serine