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Phosphorylation of CpgA protein enhances both its GTPase activity and its affinity for ribosome and is crucial for Bacillus subtilis growth and morphology.

Abstract : In Bacillus subtilis, the ribosome-associated GTPase CpgA is crucial for growth and proper morphology and was shown to be phosphorylated in vitro by the Ser/Thr protein kinase PrkC. To further understand the function of the Escherichia coli RsgA ortholog, CpgA, we first demonstrated that its GTPase activity is stimulated by its association with the 30 S ribosomal subunit. Then the role of CpgA phosphorylation was analyzed. A single phosphorylated residue, threonine 166, was identified by mass spectrometry. Phosphoablative replacement of this residue in CpgA induces a decrease of both its affinity for the 30 S ribosomal subunit and its GTPase activity, whereas a phosphomimetic replacement has opposite effects. Furthermore, cells expressing a nonphosphorylatable CpgA protein present the morphological and growth defects similar to those of a cpgA-deleted strain. Altogether, our results suggest that CpgA phosphorylation on Thr-166 could modulate its ribosome-induced GTPase activity. Given the role of PrkC in B. subtilis spore germination, we propose that CpgA phosphorylation is a key regulatory process that is essential for B. subtilis development.
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https://hal.archives-ouvertes.fr/hal-00965576
Contributor : Laurence Naiglin Connect in order to contact the contributor
Submitted on : Tuesday, March 25, 2014 - 2:00:37 PM
Last modification on : Wednesday, May 18, 2022 - 3:11:52 AM

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Frédérique Pompeo, Céline Freton, Catherine Wicker-Planquart, Christophe Grangeasse, Jean-Michel Jault, et al.. Phosphorylation of CpgA protein enhances both its GTPase activity and its affinity for ribosome and is crucial for Bacillus subtilis growth and morphology.. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (25), pp.20830-8. ⟨10.1074/jbc.M112.340331⟩. ⟨hal-00965576⟩

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