Protein arginine (de)phosphorylation

Protein arginine phosphorylation in the bacterial stress response

The reversible phosphorylation of proteins plays a critical role in regulating almost every cellular process. This remarkable regulatory impact is due to the fact that the attached phosphate group can influence the properties of the target protein in various ways. It may influence the conformation of the protein thus promoting its activation or inhibition, increase or decrease the stability of the protein, alter its localization and/or influence the interactions with other proteins. Although, most studies analyzing protein phosphorylations focus on pSer, pThr and pTyr, so-called O-phosphorylations, phosphorylation of His, Arg and Lys may constitute an equally important modification. These N-phosphorylations appear to be underrepresented in the current literature due to technical difficulties in working with them. Most notably, N-phosphorylations are unstable under acidic conditions, in contrast to O-phosphorylations, and are thus more difficult to detect by classic proteomic methods. Overcoming these limitations and further exploring possibly "overlooked" protein modification is one major research focus in our group.

In this project, we are interested in

  • identifying kinases and phosphatases that target arginine residues.
  • the respective (de)phosphorylation mechanisms.
  • the biological role of pArg in different model systems.

Projects in the lab

McsB and YwlE - in the bacterial stress response
pArg proteome analysis - revealing biological function
pArg - a degradation tag of Clp proteolytic machines