Post-translational modification of proteins by reversible phosphorylation in prokaryotes.

Microorganisms have developed three different systems for catalyzing protein phosphorylation and using this reversible modificaiton to regulate their cellular activities. The first 'classical' system utilizes nucleoside-triphosphates as phosphoryl donors and leads to the modification of protein substrates at serine/threonine or tyrosine residues. The second system, called 'two-component system', requires first a sensor kinase which autophosphorylates at a histidine residue at the expense of adenosine-triphosphate, then a response regulator which is modified in turn at an aspartate residue and thereafter induces a metabolic change within the cell. The third system, called 'PTS system', makes use of phosphoenol pyruvate to generate a phosphoryl group which is passed down a chain of several proteins and finally transferred to a sugar. There is increasing evidence that, contrary to an early concept, these systems and the corresponding enzymes (protein kinases and phosphoprotein phosphatases) share a number of structural and functional similarities with the phosphorylation-dephosphorylation machineries found in eukaryotes. Therefore one can expect that microorganisms will serve, once again, as a basic model for exploring and understanding a key regulatory mechanism, reversible protein phosphorylation, which concerns all organisms.