Phosphorylation of CpgA Protein Enhances Both Its GTPase Activity and Its Affinity for Ribosome and Is Crucial for Bacillus subtilis Growth and Morphology

Pompeo, Frédérique; Freton, Céline; Wicker‐Planquart, Catherine; Grangeasse, Christophe; Jault, Jean‐Michel; Galinier, Anne

doi:10.1074/jbc.m112.340331

Cited by 15 publications

(20 citation statements)

References 37 publications

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“…When 1 μM 50S particles was added, YsxC activity raised by a 3.7‐ to 9‐fold factor (0.33–0.83 mmol min −1 mmol −1 ). The stimulation of YsxC GTPase activity is in the same order of magnitude than the stimulation observed for HflX upon binding to the 50S (8‐fold increase for the hydrolysis of GTP [35]) but lower than that observed for 70S‐bound CpgA (50‐fold [37]). By contrast, no enhancement in YsxC activity could be detected in the presence of 30S particles.…”

Section: Resultsmentioning

confidence: 69%

“…The intrinsic GTPase activity of YsxC is very low (0.004 μmol min −1 mg −1 , or 0.09 mmol min −1 mmol −1 ), but in the same range as the one of Era from E. coli (0.01–0.02 mmol min −1 mmol −1 [36]), CpgA from B. subtilis (0.05 mmol min −1 mmol −1 [37]), or ras p21 (0.005–0.006 mmol min −1 mmol −1 , [38]). When 1 μM 50S particles was added, YsxC activity raised by a 3.7‐ to 9‐fold factor (0.33–0.83 mmol min −1 mmol −1 ).…”

Section: Resultsmentioning

confidence: 99%

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Interaction between Bacillus subtilis YsxC and ribosomes (or rRNAs)

Wicker‐Planquart

Jault

2015

FEBS Letters

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a b s t r a c tYsxC is an essential P-loop GTPase, that binds to the 50S ribosomal subunit, and is required for the proper assembly of the ribosome. The aim of this study was to characterize YsxC ribosome interactions.The stoichiometry of YsxC ribosome subunit complex was evaluated. We showed that YsxC binding to the 50S ribosomal subunit is not affected by GTP, but in the presence of GDP the stoichiometry of YsxC-ribosome is decreased. YsxC GTPase activity was stimulated upon 50S ribosomal subunit binding. In addition, it is shown for the first time that YsxC binds both 16S and 23S ribosomal RNAs.

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Section: Resultsmentioning

confidence: 69%

Section: Resultsmentioning

confidence: 99%

Interaction between Bacillus subtilis YsxC and ribosomes (or rRNAs)

Wicker‐Planquart

Jault

2015

FEBS Letters

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“…The recombinant 6His‐CpgA and 6His‐YvcK were expressed and purified as described in Pompeo et al . () and Foulquier et al . () respectively.…”

Section: Methodsmentioning

confidence: 96%

Phosphorylation of the cell division protein GpsB regulates PrkC kinase activity through a negative feedback loop in Bacillus subtilis

Pompeo

Foulquier

Serrano

et al. 2015

Molecular Microbiology

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SummaryAlthough many membrane Ser/Thr-kinases with PASTA motifs have been shown to control bacterial cell division and morphogenesis, inactivation of the Ser/Thr-kinase PrkC does not impact Bacillus subtilis cell division. In this study, we show that PrkC localizes at the division septum. In addition, three proteins involved in cell division/elongation, GpsB, DivIVA and EzrA are required for stimulating PrkC activity in vivo. We show that GpsB interacts with the catalytic subunit of PrkC that, in turn, phosphorylates GpsB. These observations are not made with DivIVA and EzrA. Consistent with the phosphorylated residue previously detected for GpsB in a high-throughput phosphoproteomic analysis of B. subtilis, we show that threonine 75 is the single PrkC-mediated phosphorylation site in GpsB. Importantly, the substitution of this threonine by a phospho-mimetic residue induces a loss of PrkC kinase activity in vivo and a reduced growth under high salt conditions as observed for gpsB and prkC null mutants. Conversely, substitution of threonine 75 by a phospho-ablative residue does not induce such growth and PrkC kinase activity defects. Altogether, these data show that proteins of the divisome control PrkC activity and thereby phosphorylation of PrkC substrates through a negative feedback loop in B. subtilis.

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“…The extracellular domain of PknB binds peptidoglycan (PG)-derived muropeptides (22), and the kinase exerts downstream effects on cell wall synthesis, cell shape, cell division, transcription, and translation (20,23,24). Similarly, the homologous Bacillus subtilis STPK PrkC has been shown to bind muropeptides that induce the germination of dormant spores, most likely by stimulating the PrkC-dependent phosphorylation of a ribosomal GTPase (25)(26)(27). Beyond this example, however, the precise environmental signals that trigger STPK signaling in bacteria are unknown, and the downstream processes regulated by these kinases are poorly defined.…”

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confidence: 99%

Osmosensory signaling in Mycobacterium tuberculosis mediated by a eukaryotic-like Ser/Thr protein kinase

Hatzios¹,

Baer

Rustad

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Significance Osmotic stress is one of many environmental hazards encountered by bacteria during the course of infection, but our understanding of how bacteria perceive and respond to changes in extracellular osmolarity is still incomplete. We show that Mycobacterium tuberculosis , the pathogen that causes tuberculosis in humans, responds, in part, through an osmosensory pathway regulated by the Ser/Thr protein kinase (STPK) PknD. Our work demonstrates that increasing extracellular osmolarity induces expression of a PknD substrate that regulates bacterial transcription, cell wall remodeling, and virulence factor production. Because STPKs are prevalent in bacteria, these proteins may play a broad role in bacterial osmosensing.

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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

Cited by 15 publications

References 37 publications

Interaction between Bacillus subtilis YsxC and ribosomes (or rRNAs)

Interaction between Bacillus subtilis YsxC and ribosomes (or rRNAs)

Phosphorylation of the cell division protein GpsB regulates PrkC kinase activity through a negative feedback loop in Bacillus subtilis

Osmosensory signaling in Mycobacterium tuberculosis mediated by a eukaryotic-like Ser/Thr protein kinase

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