@article{LilgeRederTippmannetal.2020,
  author    = {Lars Lilge and Alexander Reder and Frank Tippmann and Friedrich Morgenroth and Janice Grohmann and D{\"o}rte Becher and Katharina Riedel and Uwe V{\"o}lker and Michael Hecker and Ulf Gerth},
  title     = {The Involvement of the McsB Arginine Kinase in Clp-Dependent Degradation of the MgsR Regulator in Bacillus subtilis},
  series   = {Frontiers in Microbiology},
  volume    = {11},
  publisher = {Frontiers Media S.A.},
  issn      = {1664-302X},
  doi       = {10.3389/fmicb.2020.00900},
  url       = {https://nbn-resolving.org/urn:nbn:de:gbv:9-opus-37621},
  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.},
  language  = {en}
}