Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis b bThe primer sequences used for PCR in this study are shown as supplementary data on Microbiology Online (http://mic.sgmjournals.org).

Morimoto, Takahiro; Loh, Pek Chin; Hirai, Tadayoshi; Asai, Kei; Kobayashi, Kazuo; Moriya, Shigeki; Ogasawara, Nagahisa

doi:10.1099/00221287-148-11-3539

Cited by 166 publications

(168 citation statements)

References 64 publications

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“…RsgA from S. aureus, E. coli, and B. subtilis is a nonessential protein that is nonetheless important for normal growth (34)(35)(36), whereas both RbgA and Era are essential (37)(38)(39)(40)(41)(42). Unlike eukaryotic GTPases that have roles in membrane signaling, members of this family of prokaryotic GTPases appear to have functions linked to ribosome assembly.…”

Section: Resultsmentioning

confidence: 99%

ppGpp negatively impacts ribosome assembly affecting growth and antimicrobial tolerance in Gram-positive bacteria

Corrigan

Bellows

Wood

et al. 2016

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

187

227

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The stringent response is a survival mechanism used by bacteria to deal with stress. It is coordinated by the nucleotides guanosine tetraphosphate and pentaphosphate [(p)ppGpp], which interact with target proteins to promote bacterial survival. Although this response has been well characterized in proteobacteria, very little is known about the effectors of this signaling system in Grampositive species. Here, we report on the identification of seven target proteins for the stringent response nucleotides in the Grampositive bacterium Staphylococcus aureus. We demonstrate that the GTP synthesis enzymes HprT and Gmk bind with a high affinity, leading to an inhibition of GTP production. In addition, we identified five putative GTPases-RsgA, RbgA, Era, HflX, and ObgE-as (p)ppGpp target proteins. We show that RsgA, RbgA, Era, and HflX are functional GTPases and that their activity is promoted in the presence of ribosomes but strongly inhibited by the stringent response nucleotides. By characterizing the function of RsgA in vivo, we ascertain that this protein is involved in ribosome assembly, with an rsgA deletion strain, or a strain inactivated for GTPase activity, displaying decreased growth, a decrease in the amount of mature 70S ribosomes, and an increased level of tolerance to antimicrobials. We additionally demonstrate that the interaction of ppGpp with cellular GTPases is not unique to the staphylococci, as homologs from Bacillus subtilis and Enterococcus faecalis retain this ability. Taken together, this study reveals ribosome inactivation as a previously unidentified mechanism through which the stringent response functions in Gram-positive bacteria.ribosome | stringent response | tolerance | ppGpp | Staphylococcus aureus

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Section: Resultsmentioning

confidence: 99%

ppGpp negatively impacts ribosome assembly affecting growth and antimicrobial tolerance in Gram-positive bacteria

Corrigan

Bellows

Wood

et al. 2016

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

187

227

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“…Both YlqF and YqeH are essential for cell growth in Bacillus subtilis. They have been shown to bind [␣- 32 P]GTP (31), and GTPase activity was demonstrated for YqeH (32). The B. subtilis yqeH mutant is lethal, whereas reduced YqeH expression increases chromosomal replication (31).…”

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confidence: 99%

“…They have been shown to bind [␣- 32 P]GTP (31), and GTPase activity was demonstrated for YqeH (32). The B. subtilis yqeH mutant is lethal, whereas reduced YqeH expression increases chromosomal replication (31). YqeH participates in the biogenesis of the 30 S ribosome subunit (32) and assists in 50 S ribosome assembly (33).…”

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confidence: 99%

The Structure of YqeH

Sudhamsu

Lee

Klessig

et al. 2008

Journal of Biological Chemistry

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AtNOS1/AtNOA1 was identified as a nitric oxide-generating enzyme in plants, but that function has recently been questioned. To resolve issues surrounding AtNOA1 activity, we report the biochemical properties and a 2.36 Å resolution crystal structure of a bacterial AtNOA1 ortholog (YqeH). Geobacillus YqeH fused to a putative AtNOA1 leader peptide complements growth and morphological defects of Atnoa1 mutant plants. YqeH does not synthesize nitric oxide from L-arginine but rather hydrolyzes GTP. The YqeH structure reveals a circularly permuted GTPase domain and an unusual C-terminal ␤-domain. A small N-terminal domain, disordered in the structure, binds zinc. Structural homology among the C-terminal domain, the RNA-binding regulator TRAP, and the hypoxia factor pVHL define a recognition module for peptides and nucleic acids. TRAP residues important for RNA binding are conserved by the YqeH C-terminal domain, whose positioning is coupled to GTP hydrolysis. YqeH and AtNOA1 probably act as G-proteins that regulate nucleic acid recognition and not as nitric-oxide synthases.

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“…GTPases control a wide variety of biological processes, including protein synthesis and cell cycle control. Most bacteria generally encode several highly conserved GTP-binding proteins of unknown function (at least 11 in B. subtilis), many of which are essential for growth (Morimoto et al, 2002). The last gene of the locus, lmo1273, encodes a putative RNase HII of 261 amino acids, sharing 51 % amino acid identity with the rnhB-encoded RNase HII of B. subtilis.…”

Section: Results Lmo1273 Encodes An Rnase H Homologuementioning

confidence: 99%

lmo1273, a novel gene involved in Listeria monocytogenes virulence

et al. 2009

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Listeria monocytogenes is a foodborne pathogen able to infect humans and many other mammalian species, leading to serious, often fatal disease. We have previously identified a five-gene locus in the genome of L. monocytogenes EGD-e which comprised three contiguous genes encoding paralogous type I signal peptidases. In the present study, we focused on the two distal genes of the locus (lmo1272 and lmo1273), encoding proteins sharing significant similarities with the YlqF and RnhB proteins, respectively, of Bacillus subtilis. lmo1273 could complement an Escherichia coli rnhA-rnhB thermosensitive growth phenotype, suggesting that it encodes a functional RNase H. Strikingly, inactivation of lmo1273 provoked a strong attenuation of virulence in the mouse model, and kinetic studies in infected mice revealed that multiplication of the lmo1273 mutant in target organs was significantly impaired. However, the mutation did not impair L. monocytogenes intracellular multiplication or cell-to-cell spread in cell culture models. Transcriptional profiles obtained with an lmo1273-overexpressing strain were compared to those of the wild-type strain, using microarray analyses. The data obtained suggest a pleiotropic regulatory role of Lmo1273 and possible links with amino acid uptake.

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Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis b bThe primer sequences used for PCR in this study are shown as supplementary data on Microbiology Online (http://mic.sgmjournals.org).

Cited by 166 publications

References 64 publications

ppGpp negatively impacts ribosome assembly affecting growth and antimicrobial tolerance in Gram-positive bacteria

ppGpp negatively impacts ribosome assembly affecting growth and antimicrobial tolerance in Gram-positive bacteria

The Structure of YqeH

lmo1273, a novel gene involved in Listeria monocytogenes virulence

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