@article{LilgeRederTippmannetal.2020,
  author    = {Lilge, Lars and Reder, Alexander and Tippmann, Frank and Morgenroth, Friedrich and Grohmann, Janice and Becher, D{\"o}rte and Riedel, Katharina and V{\"o}lker, Uwe and Hecker, Michael and Gerth, Ulf},
  title     = {The Involvement of the McsB Arginine Kinase in Clp-Dependent Degradation of the MgsR Regulator in Bacillus subtilis},
  journal   = {Frontiers in Microbiology},
  volume    = {11},
  issn      = {1664-302X},
  doi       = {10.3389/fmicb.2020.00900},
  institution = {Institut f{\"u}r Mikrobiologie - Abteilung f{\"u}r Genetik \& Biochemie},
  year      = {2020},
  abstract  = {Regulated ATP-dependent proteolysis is a common feature of developmental processes and plays also a crucial role during environmental perturbations such as stress and starvation. The Bacillus subtilis MgsR regulator controls a subregulon within the stress- and stationary phase σB regulon. After ethanol exposition and a short time-window of activity, MgsR is ClpXP-dependently degraded with a half-life of approximately 6 min. Surprisingly, a protein interaction analysis with MgsR revealed an association with the McsB arginine kinase and an in vivo degradation assay confirmed a strong impact of McsB on MgsR degradation. In vitro phosphorylation experiments with arginine (R) by lysine (K) substitutions in McsB and its activator McsA unraveled all R residues, which are essentially needed for the arginine kinase reaction. Subsequently, site directed mutagenesis of the MgsR substrate was used to substitute all arginine residues with glutamate (R-E) to mimic arginine phosphorylation and to test their influence on MgsR degradation in vivo. It turned out, that especially the R33E and R94/95E residues (RRPI motif), the latter are adjacently located to the two redox-sensitive cysteines in a 3D model, have the potential to accelerate MgsR degradation. These results imply that selective arginine phosphorylation may have favorable effects for Clp dependent degradation of short-living regulatory proteins. We speculate that in addition to its kinase activity and adaptor function for the ClpC ATPase, McsB might also serve as a proteolytic adaptor for the ClpX ATPase in the degradation mechanism of MgsR.},
  subject      = {-},
  language  = {en}
}