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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.

Abstract : 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.
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https://hal.archives-ouvertes.fr/hal-00594193
Contributor : Marie-Claude Serre Connect in order to contact the contributor
Submitted on : Thursday, May 19, 2011 - 10:52:36 AM
Last modification on : Friday, January 21, 2022 - 3:26:21 AM

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Cédric Absalon, Michal Obuchowski, Edwige Madec, Delphine Delattre, I Barry Holland, et al.. CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis.. Microbiology, Microbiology Society, 2009, 155 (Pt 3), pp.932-43. ⟨10.1099/mic.0.022475-0⟩. ⟨hal-00594193⟩

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