PrkC-mediated phosphorylation of overexpressed YvcK protein regulates PBP1 protein localization in Bacillus subtilis mreB mutant cells.

@article{Foulquier2014PrkCmediatedPO,
  title={PrkC-mediated phosphorylation of overexpressed YvcK protein regulates PBP1 protein localization in Bacillus subtilis mreB mutant cells.},
  author={Elodie Foulquier and Fr{\'e}d{\'e}rique Pompeo and C{\'e}line Freton and Baptiste Cordier and Christophe Grangeasse and Anne Galinier},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 34},
  pages={
          23662-9
        }
}
The YvcK protein has been shown to be necessary for growth under gluconeogenic conditions in Bacillus subtilis. Amazingly, its overproduction rescues growth and morphology defects of the actin-like protein MreB deletion mutant by restoration of PBP1 localization. In this work, we observed that YvcK was phosphorylated at Thr-304 by the protein kinase PrkC and that phosphorylated YvcK was dephosphorylated by the cognate phosphatase PrpC. We show that neither substitution of this threonine with a… CONTINUE READING
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