The Growth-Promoting and Stress Response Activities of the
            <i>Bacillus subtilis</i>
            GTP Binding Protein Obg Are Separable by Mutation

Kuo, Shrin; Demeler, Borries; Haldenwang, W G

doi:10.1128/jb.00799-08

Cited by 29 publications

(51 citation statements)

References 56 publications

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“…the N-terminal (Jiang et al, 2007) or the C-terminal of ObgE (this work)). Recent work in Bacillus subtilis suggests that the N-terminal domain is involved in Obg’s growth phenotype whereas its C-terminal domain is involved with stress responses (Kuo et al, 2008). Although the C-terminal Tn 5 mutant could either increase or decrease overall (p)ppGpp levels through hypothetical misregulation of SpoT, we note that the observed phenotypes of the mutant with respect to replication --slow to arrest and slow to resume-- is consistent with neither scenario.…”

Section: Discussionmentioning

confidence: 99%

The ObgE/CgtA GTPase influences the stringent response to amino acid starvation in Escherichia coli

Persky

Ferullo

Cooper

et al. 2009

Molecular Microbiology

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SummaryThe stringent response is important for bacterial survival under stressful conditions, such as amino acid starvation, and is characterized by the accumulation of ppGpp and pppGpp. ObgE (CgtA, YhbZ) is an essential conserved GTPase in Escherichia coli and several observations have implicated the protein in the control of the stringent response. However, consequences of the protein on specific responses to amino acid starvation have not been noted. We show that ObgE binds to ppGpp with biologically relevant affinity in vitro, implicating ppGpp as an in vivo ligand of ObgE. ObgE mutants increase the ratio of pppGpp to ppGpp within the cell during the stringent response. These changes are correlated with a delayed inhibition of DNA replication by the stringent response, delayed resumption of DNA replication after release, as well as a decreased survival after amino acid deprivation. With these data, we place ObgE as an active effector of the response to amino acid starvation in vivo. Our data correlate the pppGpp/ppGpp ratio with DNA replication control under bacterial starvation conditions, suggesting a possible role for the relative balance of these two nucleotides.

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Section: Discussionmentioning

confidence: 99%

The ObgE/CgtA GTPase influences the stringent response to amino acid starvation in Escherichia coli

Persky

Ferullo

Cooper

et al. 2009

Molecular Microbiology

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“…The B. subtilis Nterminal domain dimerizes just as do other heme-liganded globin sensor proteins of bacteria [17]. By analogy with mammalian neuroglobin's hypoxia signaling through inhibition of GTP-GDP exchange by heterotrimeric G proteins, the N-terminal domain of RbsR may modify in a stress-dependent fashion the binding of ribosomeassociated, low-affinity GTPase Obg [18] (not shown in Fig. 2A) to the kinase RsbT.…”

Section: Stas Domain Proteins Of the Stressosomementioning

confidence: 99%

STAS Domain Structure and Function

Sharma¹,

Rigby²,

Alper³

2011

Cell Physiol Biochem

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Pendrin shares with nearly all SLC26/SulP anion transporters a carboxy-terminal cytoplasmic segment organized around a Sulfate Transporter and Anti-Sigma factor antagonist (STAS) domain. STAS domains of divergent amino acid sequence exhibit a conserved fold of 4 β strands interspersed among 5 α helices. The first STAS domain proteins studied were single-domain anti-sigma factor antagonists (anti-anti-σ). These anti-anti-σ indirectly stimulate bacterial RNA polymerase by inactivating inhibitory anti-σ kinases, liberating σ factors to direct specific transcription of target genes or operons. Some STAS domains are nucleotide-binding phosphoproteins or nucleotidases. Others are interaction/transduction modules within multidomain sensors of light, oxygen and other gasotransmitters, cyclic nucleotides, inositol phosphates, and G proteins. Additional multidomain STAS protein sequences suggest functions in sensing, metabolism, or transport of nutrients such as sugars, amino acids, lipids, anions, vitamins, or hydrocarbons. Still other multidomain STAS polypeptides include histidine and serine/threonine kinase domains and ligand-activated transcription factor domains. SulP/SLC26 STAS domains and adjacent sequences interact with other transporters, cytoskeletal scaffolds, and with enzymes metabolizing transported anion substrates, forming putative metabolons. STAS domains are central to membrane targeting of many SulP/SLC26 anion transporters, and STAS domain mutations are associated with at least three human recessive diseases. This review summarizes STAS domain structure and function.

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“…21). However, the GTP-binding and hydrolase activities of SpoIIAA (22) have unclear physiological functions, and no known relationship to either sporulation or the growth-promoting functions of the ribosome-associated GTPase, Obg (23).…”

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confidence: 99%

Solution Structure of the Guanine Nucleotide-binding STAS Domain of SLC26-related SulP Protein Rv1739c from Mycobacterium tuberculosis

Sharma

Baer

et al. 2011

Journal of Biological Chemistry

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The structure and intrinsic activities of conserved STAS domains of the ubiquitous SulP/SLC26 anion transporter superfamily have until recently remained unknown. Here we report the heteronuclear, multidimensional NMR spectroscopy solution structure of the STAS domain from the SulP/SLC26 putative anion transporter Rv1739c of Mycobacterium tuberculosis. The 0.87-Å root mean square deviation structure revealed a four-stranded ␤-sheet with five interspersed ␣-helices, resembling the anti-factor antagonist fold. Rv1739c STAS was shown to be a guanine nucleotide-binding protein, as revealed by nucleotide-dependent quench of intrinsic STAS fluorescence and photoaffinity labeling. NMR chemical shift perturbation analysis partnered with in silico docking calculations identified solvent-exposed STAS residues involved in nucleotide binding. Rv1739c STAS was not an in vitro substrate of mycobacterial kinases or anti-factors. These results demonstrate that Rv1739c STAS binds guanine nucleotides at physiological concentrations and undergoes a ligand-induced conformational change but, unlike anti-factor antagonists, may not mediate signals via phosphorylation.

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The Growth-Promoting and Stress Response Activities of the Bacillus subtilis GTP Binding Protein Obg Are Separable by Mutation

Cited by 29 publications

References 56 publications

The ObgE/CgtA GTPase influences the stringent response to amino acid starvation in Escherichia coli

The ObgE/CgtA GTPase influences the stringent response to amino acid starvation in Escherichia coli

STAS Domain Structure and Function

Solution Structure of the Guanine Nucleotide-binding STAS Domain of SLC26-related SulP Protein Rv1739c from Mycobacterium tuberculosis

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