Phosphorylation in the Archaeon Halobacterium salinarum
Author Information
Author(s): Aivaliotis Michalis, Macek Boris, Gnad Florian, Reichelt Peter, Mann Matthias, Oesterhelt Dieter
Primary Institution: Max Planck Institute of Biochemistry, Martinsried, Germany
Hypothesis
Archaea, like eukaryotes, utilize Ser/Thr/Tyr phosphorylation for protein regulation.
Conclusion
The study identifies 90 unique phosphopeptides from 69 proteins in Halobacterium salinarum, demonstrating the presence of Ser/Thr/Tyr phosphorylation in archaea.
Supporting Evidence
- 90 unique phosphopeptides from 69 proteins were identified.
- Phosphorylation was found to be involved in various cellular processes.
- The study provides the largest set of archaeal proteins phosphorylated on Ser/Thr/Tyr residues to date.
- Phosphorylation is suggested to play a fundamental regulatory role in archaea.
Takeaway
Scientists found that a tiny organism called Halobacterium salinarum can change its proteins using a special process called phosphorylation, just like more complex life forms do.
Methodology
Genome-wide, gel-free, and site-specific phosphoproteome analysis using high accuracy mass spectrometry.
Limitations
Only a limited number of archaeal phosphoproteins have been identified, and the functional roles of many remain unknown.
Digital Object Identifier (DOI)
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