Non-enzymatic Ser/Thr/Tyr phosphorylation: a new player in bacterial protein phosphorylation?

Post-translational modifications are covalent and often enzymatic modification of a protein after its synthesis. Protein Ser/Thr/Tyr phosphorylation is one of the most important and well understood post-translational modifications. The current understanding is that dedicated proteins (kinases and phosphatases) add and remove a phosphate moiety to the –OH group of Ser, Thr, or Tyr residues thus affecting protein function. There is however a large discrepancy between the number of phosphoproteins and the kinases supposed to phosphorylate them in bacteria. In this project I will challenge the deeply-rooted belief that only kinases can phosphorylate proteins. The project thus holds potential of providing an answer to a long-standing question how kinases can be able to phosphorylate many structurally diverse substrates and still retain high specificity by correcting a long-standing misconception in the field, namely that protein phosphorylation is catalysed exclusively by kinases.