Abstract
Protein phosphorylation in serine, threonine and tyrosine residues is a central paradigm in cell signaling. However, in prokaryotes this post-translational modification (PTM) was dismissed until last two decades. Several bacterial phosphoproteomic studies along with identification and characterization of the enzymes responsible of protein phosphorylation in these organisms, has triggered a fresh view on the research area pointing out to this PTM as an important regulatory mechanism in bacteria. Particularly, in this review we will focus on tyrosine phosphorylation, the kinases and phosphatases achieving incorporation and removal of phosphate moiety, and their mechanism of action and impact on the bacterial physiology.
TIP Magazine Specialized in Chemical-Biological Sciences, distributed under Creative Commons License: Attribution + Noncommercial + NoDerivatives 4.0 International.