Protein Ser/Thr/Tyr phosphorylation in the Archaea

J Biol Chem. 2014 Apr 4;289(14):9480-7. doi: 10.1074/jbc.R113.529412. Epub 2014 Feb 19.

Abstract

The third domain of life, the Archaea (formerly Archaebacteria), is populated by a physiologically diverse set of microorganisms, many of which reside at the ecological extremes of our global environment. Although ostensibly prokaryotic in morphology, the Archaea share much closer evolutionary ties with the Eukarya than with the superficially more similar Bacteria. Initial genomic, proteomic, and biochemical analyses have revealed the presence of "eukaryotic" protein kinases and phosphatases and an intriguing set of serine-, threonine-, and tyrosine-phosphorylated proteins in the Archaea that may offer new insights into this important regulatory mechanism.

Keywords: Archaea; Archaebacteria; Evolution; Protein Kinases; Protein Phosphatase; Protein Phosphorylation.

Publication types

  • Review

MeSH terms

  • Archaea / enzymology*
  • Archaea / genetics
  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism*
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*

Substances

  • Archaeal Proteins
  • Protein Serine-Threonine Kinases