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CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis

Cédric Absalon^1,

Edwige Madec^1,

Delphine Delattre^1,

¹ Université Paris-Sud 11, CNRS UMR 8621, Institut de Génétique et Microbiologie, 91405 Orsay, France
² Medical University of Gdansk, Debinki 1, 80-211, Department of Medical Biotechnology, Intercollegiate Faculty of Biotechnology, Gdansk, Poland

Correspondence
Simone J. Séror
simone.seror{at}igmors.u-psud.fr

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.

Present address: Children's Hospital Boston/Harvard Medical School, Division of Infectious Disease, Boston, MA 02115, USA.

Present address: Université des Sciences et Technologies de Lille, Unité de Glycobiologie Structurale et Fonctionnelle, UMR CNRS/USTL no. 8576, Bâtiment C9, 59655 Villeneuve d'Ascq cedex, France.

Present address: Antagene, 2 allée des Séquoias, 69760 Limonest, France.

A supplementary table of primers is available with the online version of this paper.

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