title: The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells.
abstract: Loss of the PrpC serine-threonine phosphatase and the associated PrkC kinase of Bacillus subtilis were shown to have opposite effects on stationary-phase physiology by differentially affecting cell density, cell viability, and accumulation of beta-galactosidase from a general stress reporter fusion. These pleiotropic effects suggest that PrpC and PrkC have important regulatory roles in stationary-phase cells. Elongation factor G (EF-G) was identified as one possible target of the PrpC and PrkC pair in vivo, and purified PrpC and PrkC manifested the predicted phosphatase and kinase activities against EF-G in vitro.
authors.affiliation: Department of Food Science and Technology, University of California, Davis 95616, USA.
authors.forename: Tatiana A
authors.initials: TA
authors.lastname: Gaidenko
authors.forename: Tae-Jong
authors.initials: TJ
authors.lastname: Kim
authors.forename: Chester W
authors.initials: CW
authors.lastname: Price
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology / Q000254:growth & development* / Q000502:physiology; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D015169:Colony Count, Microbial; D015964:Gene Expression Regulation, Bacterial; D009154:Mutation; D020653:Peptide Elongation Factor G / Q000378:metabolism; D010641:Phenotype; D010749:Phosphoprotein Phosphatases / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000235:genetics / Q000378:metabolism*; D001616:beta-Galactosidase / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D020653:Peptide Elongation Factor G; D011493:Protein Kinase C; D010749:Phosphoprotein Phosphatases; D001616:beta-Galactosidase