ArticleThe Journal of biological chemistry2012
Phosphorylation of CpgA protein enhances both its GTPase activity and its affinity for ribosome and is crucial for Bacillus subtilis growth and morphology.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- AJournal of bacteriology · 2025Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- Structural, Metabolic and Evolutionary Comparison of Bacterial Endospore and Exospore Formation.Frontiers in microbiology · 2021Review
- Protein post-translational modifications in bacteria.Nature reviews. Microbiology · 2019Review
- A bacterial checkpoint protein for ribosome assembly moonlights as an essential metabolite-proofreading enzyme.Nature communications · 2019Article
- Dual regulation of activity and intracellular localization of the PASTA kinase PrkC during Bacillus subtilis growth.Scientific reports · 2018Article
- Impact of Serine/Threonine Protein Kinases on the Regulation of Sporulation in Bacillus subtilis.Frontiers in microbiology · 2016Review
- The Eukaryotic-Like Ser/Thr Kinase PrkC Regulates the Essential WalRK Two-Component System in Bacillus subtilis.PLoS genetics · 2015Article
- Ser/Thr phosphorylation as a regulatory mechanism in bacteria.Current opinion in microbiology · 2015Review
- PrkC-mediated phosphorylation of overexpressed YvcK protein regulates PBP1 protein localization in Bacillus subtilis mreB mutant cells.The Journal of biological chemistry · 2014Article
- Osmosensory signaling in Mycobacterium tuberculosis mediated by a eukaryotic-like Ser/Thr protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Bacillus subtilis serine/threonine protein kinase YabT is involved in spore development via phosphorylation of a bacterial recombinase.Molecular microbiology · 2013Article
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6 authors.
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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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