The
            <i>Bacillus subtilis</i>
            GTP Binding Protein Obg and Regulators of the ς
            <sup>B</sup>
            Stress Response Transcription Factor Cofractionate with Ribosomes

Scott, Janelle M.; Ju, Jingliang; Mitchell, Theresa; Haldenwang, W G

doi:10.1128/jb.182.10.2771-2777.2000

Cited by 103 publications

(150 citation statements)

References 43 publications

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“…YlqF Is Specifically Associated with the 50 S Ribosomal Subunit-Era, Obg, and YjeQ interact with ribosomal subunits in various bacteria (17)(18)(19)(20)(21)(22)27). Accordingly, we examined whether the essential GTPbinding proteins (Era, Obg, YsxC, YlqF, YphC, and YqeH) in B. subtilis are associated with the ribosome.…”

Section: Resultsmentioning

confidence: 99%

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The GTP-binding Protein YlqF Participates in the Late Step of 50 S Ribosomal Subunit Assembly in Bacillus subtilis

Matsuo

Morimoto²,

Kuwano

et al. 2006

Journal of Biological Chemistry

111

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Bacillus subtilis YlqF belongs to the Era/Obg subfamily of small GTP-binding proteins and is essential for bacterial growth. Here we report that YlqF participates in the late step of 50 S ribosomal subunit assembly. YlqF was co-fractionated with the 50 S subunit, depending on the presence of noncleavable GTP analog. Moreover, the GTPase activity of YlqF was stimulated specifically by the 50 S subunit in vitro. Dimethyl sulfate footprinting analysis disclosed that YlqF binds to a unique position in 23 S rRNA. Yeast two-hybrid data revealed interactions between YlqF and the B. subtilis L25 protein (Ctc). The interaction was confirmed by the pull-down assay of the purified proteins. Specifically, YlqF is positioned around the A-site and P-site on the 50 S subunit. Proteome analysis of the abnormal 50 S subunits that accumulated in YlqF-depleted cells showed that L16 and L27 proteins, located near the YlqF-binding domain, are missing. Our results collectively indicate that YlqF will organize the late step of 50 S ribosomal subunit assembly.

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Section: Resultsmentioning

confidence: 99%

“…Obg interacts with the 50 S subunit in E. coli and Caulobacter crescentus (17,18). In Bacillus subtilis, Obg cofractionates with the 50 S subunit and specifically interacts with the ribosomal protein, L13 (19). In contrast, E. coli Era interacts with the 30 S subunit (20,21,22).…”

mentioning

confidence: 99%

The GTP-binding Protein YlqF Participates in the Late Step of 50 S Ribosomal Subunit Assembly in Bacillus subtilis

Matsuo

Morimoto²,

Kuwano

et al. 2006

Journal of Biological Chemistry

111

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“…This is probably a conserved function because in other organisms, such as V. harveyi, B. subtilis, C. crescentus, and E. coli, CgtA interacts with the 50S ribosomal subunit and has been shown to be involved in assembly or stability of the 50S subunit (17,23,27,28). Interestingly, a yeast mitochondrial CgtA homolog is essential for translation, likely through an involvement in ribosome biogenesis (29).…”

mentioning

confidence: 99%

“…CgtA/Obg proteins interact with components of the stress response pathways in B. subtilis and E. coli. In B. subtilis, Obg interacts with the general stress response pathway and is necessary for activation of the stress resistance transcription factor, B , which is induced by both nutritional and physical stress (23). In E. coli, CgtA interacts with SpoT (24).…”

mentioning

confidence: 99%

Regulation of the stringent response is the essential function of the conserved bacterial G protein CgtA in Vibrio cholerae

Raskin

Judson²,

Mekalanos³

2007

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

107

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The gene encoding the conserved bacterial G protein CgtA (Obg) is essential for viability in every organism in which it has been studied. CgtA has been reported to be involved in several diverse bacterial functions, including ribosome assembly, DNA repair, sporulation, and morphological development. However, none of these functions have been identified as essential. Here we show that depletion of CgtA in Vibrio cholerae causes global changes in gene expression that are consistent with induction of a classical low nutrient stress response or ''stringent'' response. We show that depletion of CgtA leads to increased ppGpp levels that correlate with induction of the global stress response and cessation of growth. The enzyme RelA is responsible for synthesis of the alarmone ppGpp during the stringent response. We show that CgtA is no longer essential in a relA deletion mutant and thus conclude that the essentiality of CgtA is directly linked to its ability to affect ppGpp levels. The enzyme SpoT degrades ppGpp, and here we show that SpoT is essential in a RelA؉ CgtA؉ background but not in a relA deletion mutant. We also confirmed that CgtA interacts with SpoT in a two-hybrid assay. We suggest that the essential function of CgtA is as a repressor of the stringent response that acts by regulating SpoT activity to maintain low ppGpp levels when bacteria are growing in a nutrient-rich environment.alarmone ͉ cholera ͉ GTPase ͉ starvation ͉ transcription

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“…The other motifs indicate GTP binding, GTPase, methyltransferase, peptidyl-prolyl isomerase, helicase activities, and chaperone function. These proteins may have roles in ribosome maturation or assembly, RNA folding, rRNA processing, protein assembly, and subunit structure stabilization similar to what has been observed in other organisms (41)(42)(43)(44)(45)(46)(47)(48)(49). Intriguingly helicase activity was recently identified in ribosomes that could account for its ability to translate through downstream mRNA secondary structure (50).…”

Section: Sequence Characteristics Of Mt Ribosomal Proteins-mostmentioning

confidence: 99%

Trypanosoma brucei Mitochondrial Ribosomes

Zı́ková

Panigrahi

Dalley

et al. 2008

Molecular & Cellular Proteomics

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Although eukaryotic mitochondrial (mt) ribosomes evolved from a putative prokaryotic ancestor their compositions vary considerably among organisms. We determined the protein composition of tandem affinity-purified Trypanosoma brucei mt ribosomes by mass spectrometry and identified 133 proteins of which 77 were associated with the large subunit and 56 were associated with the small subunit. Comparisons with bacterial and mammalian mt ribosomal proteins identified T. brucei mt homologs of L2-4, L7/12, L9, L11, L13-17, L20 -24, L27-30, L33, L38, L43, L46, L47, L49, L52, S5, S6, S8, S9, S11, S15-18, S29, and S34, although the degree of conservation varied widely. Sequence characteristics of some of the component proteins indicated apparent functions in rRNA modification and processing, protein assembly, and mitochondrial metabolism implying possible additional roles for these proteins. Nevertheless most of the identified proteins have no homology outside Kinetoplastida implying very low conservation and/or a divergent function in kinetoplastid mitochondria. Molecular & Cellular Proteomics 7:1286 -1296, 2008. Mt1 ribosomes appear to be structurally variable to a considerable extent from one organism to another and have undergone some major remodeling during their evolution including loss of RNA and acquisition of proteins (1, 2). Their sedimentation coefficient (S) values vary between 50 S in Leishmania, 70 -74 S in fungi, 55 S in metazoans, and 78 S in higher plants (3-6). Tandem mass spectrometry has been successfully applied to the analysis of the protein composition of ribosomes from several organelles including bovine mitochondria (5, 7-10), fungal mitochondria (11, 12), and chloroplasts (13,14). Mammalian ribosomes have about the same mass as bacterial ribosomes but half as much RNA and over twice as much proteins. Proteomics analysis of bovine mt ribosomes (9, 10) identified 78 different proteins, which include homologs of Escherichia coli ribosomal proteins and 36 additional proteins that presumably were acquired during eukaryotic evolution. Many of these new ribosomal proteins are distinct, having no closely related homologs in bacterial or eukaryotic cytoplasmic ribosomes. The estimated number of proteins within mammalian mt ribosomes has ranged from about 85 to more than 100, for yeast mitochondria it is 78 proteins, and for chloroplast mitochondria it is 49 proteins. The feature of protein richness implies that the reduced rRNA sizes are compensated by some protein components that might have been recruited to mt ribosomes during the course of evolution (15).Trypanosoma and Leishmania are protozoan parasites belonging to the order Kinetoplastida that are the causative agents of several devastating tropical diseases such as African sleeping sickness, Chagas disease, and leishmaniasis. Protein synthesis in the mitochondria of these unicellular flagellates has unusual features. The transcripts from most genes encoded in the trypanosomatid mt DNA are posttranscriptionally modified via extensive and precise ins...

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The Bacillus subtilis GTP Binding Protein Obg and Regulators of the ς ^B Stress Response Transcription Factor Cofractionate with Ribosomes

Cited by 103 publications

References 43 publications

The GTP-binding Protein YlqF Participates in the Late Step of 50 S Ribosomal Subunit Assembly in Bacillus subtilis

The GTP-binding Protein YlqF Participates in the Late Step of 50 S Ribosomal Subunit Assembly in Bacillus subtilis

Regulation of the stringent response is the essential function of the conserved bacterial G protein CgtA in Vibrio cholerae

Trypanosoma brucei Mitochondrial Ribosomes

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The Bacillus subtilis GTP Binding Protein Obg and Regulators of the ς B Stress Response Transcription Factor Cofractionate with Ribosomes

Cited by 103 publications

References 43 publications

The GTP-binding Protein YlqF Participates in the Late Step of 50 S Ribosomal Subunit Assembly in Bacillus subtilis

The GTP-binding Protein YlqF Participates in the Late Step of 50 S Ribosomal Subunit Assembly in Bacillus subtilis

Regulation of the stringent response is the essential function of the conserved bacterial G protein CgtA in Vibrio cholerae

Trypanosoma brucei Mitochondrial Ribosomes

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The Bacillus subtilis GTP Binding Protein Obg and Regulators of the ς ^B Stress Response Transcription Factor Cofractionate with Ribosomes