CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis.
The conserved prpC, prkC, cpgA locus in Bacillus subtilis encodes respectively a Ser/Thr phosphatase, the cognate sensor kinase (containing an external PASTA domain suggested to bind peptidoglycan precursors) and CpgA, a small ribosome-associated GTPase that we have shown previously is implicated in shape determination and peptidoglycan deposition. In this study, in a search for targets of PrkC and PrpC, we showed that, in vitro, CpgA itself is phosphorylated on serine and threonine, and another GTPase, the translation factor EF-Tu, is also phosphorylated by the kinase on the conserved T384 residue. Both substrates are dephosphorylated by PrpC in vitro. In addition, we identified YezB, a 10.3 kDa polypeptide, and a component of the stressosome, as a substrate for both enzymes in vitro and apparently in vivo. We propose that the PrpC/PrkC/CpgA system constitutes an important element of a regulatory network involved in the coordination of cell wall expansion and growth in B. subtilis.
Absalon
Cédric
C
Université Paris-Sud 11, CNRS UMR 8621, Institut de Génétique et Microbiologie, 91405 Orsay, France.
Obuchowski
Michal
M
Medical University of Gdansk, Debinki 1, 80-211, Department of Medical Biotechnology, Intercollegiate Faculty of Biotechnology, Gdansk, Poland.
Madec
Edwige
E
Université Paris-Sud 11, CNRS UMR 8621, Institut de Génétique et Microbiologie, 91405 Orsay, France.
Delattre
Delphine
D
Université Paris-Sud 11, CNRS UMR 8621, Institut de Génétique et Microbiologie, 91405 Orsay, France.
Holland
I Barry
IB
Université Paris-Sud 11, CNRS UMR 8621, Institut de Génétique et Microbiologie, 91405 Orsay, France.
Séror
Simone J
SJ
Université Paris-Sud 11, CNRS UMR 8621, Institut de Génétique et Microbiologie, 91405 Orsay, France.
D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D016297:Mutagenesis, Site-Directed; D010444:Peptide Elongation Factor Tu / Q000235:genetics / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D012694:Serine / Q000378:metabolism; D013379:Substrate Specificity; D013912:Threonine / Q000378:metabolism
D001426:Bacterial Proteins; D013912:Threonine; D012694:Serine; D017346:Protein Serine-Threonine Kinases; D010749:Phosphoprotein Phosphatases; D010444:Peptide Elongation Factor Tu