Stringent response in <i>Vibrio cholerae</i>: genetic analysis of <i>spoT</i> gene function and identification of a novel (p)ppGpp synthetase gene

Das, Bhabatosh; Pal, Ritesh Ranjan; Bag, Satyabrata; Bhadra, Rupak K.

doi:10.1111/j.1365-2958.2009.06653.x

Cited by 71 publications

(107 citation statements)

References 41 publications

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“…This phenotype is due to an additional ppGpp synthase in V. cholerae, RelV (19). The level of ppGpp accumulation was higher in the ⌬relA ⌬spoT double mutant when compared with that in wild type N16961 (Fig.…”

Section: Discussionmentioning

confidence: 94%

“…In Gram-negative bacteria, the intracellular level of ppGpp is modulated by RelA (monofunctional synthetase) and SpoT (bifunctional synthetase-hydrolase) (18). Apart from the relA and spoT genes, the novel gene relV has been identified in V. cholerae, the product of which has been shown to be involved in ppGpp synthesis under glucose or fatty acid starvation in a ⌬relA ⌬spoT double mutant (19). CgtA, the conserved bacterial GTP-binding protein, is an essential protein and has been shown to interact with SpoT in V. cholerae and Escherichia coli.…”

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confidence: 99%

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Cholera Toxin Production during Anaerobic Trimethylamine N-Oxide Respiration Is Mediated by Stringent Response in Vibrio cholerae

Park

Yoon

et al. 2014

Journal of Biological Chemistry

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Background: Cholera toxin (CT) production is induced during anaerobic respiration with trimethylamine N-oxide (TMAO) in Vibrio cholerae. Results: A bacterial stringent response to nutrient starvation was activated during anaerobic TMAO respiration and influenced CT production. Conclusion: CT production during anaerobic TMAO respiration is mediated by stringent response in V. cholerae. Significance: A mechanism of TMAO-stimulated CT production is uncovered.

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Section: Discussionmentioning

confidence: 94%

mentioning

confidence: 99%

Cholera Toxin Production during Anaerobic Trimethylamine N-Oxide Respiration Is Mediated by Stringent Response in Vibrio cholerae

Park

Yoon

et al. 2014

Journal of Biological Chemistry

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“…The identification of these small (p)ppGpp synthetase enzymes in Gram-positive bacteria reinvigorated the scientific interest in this fundamental stress response pathway. As a result, recent bioinformatic and genetic analysis indicated that single-domain (p)ppGpp-synthesizing and -hydrolysing enzymes can be found, alone or in combination, in a number of organisms, including archaea, bacteria, plants and animals (Atkinson et al, 2011;Das et al, 2009;Sun et al, 2010).…”

Section: S Mutans Is the Bacterial Paradigm Of Lactic Acid Bacteria mentioning

confidence: 99%

Streptococcus mutans: a new Gram-positive paradigm?

et al. 2013

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Despite the enormous contributions of the bacterial paradigms Escherichia coli and Bacillus subtilis to basic and applied research, it is well known that no single organism can be a perfect representative of all other species. However, given that some bacteria are difficult, or virtually impossible, to cultivate in the laboratory, that some are recalcitrant to genetic and molecular manipulation, and that others can be extremely dangerous to manipulate, the use of model organisms will continue to play an important role in the development of basic research. In particular, model organisms are very useful for providing a better understanding of the biology of closely related species. Here, we discuss how the lifestyle, the availability of suitable in vitro and in vivo systems, and a thorough understanding of the genetics, biochemistry and physiology of the dental pathogen Streptococcus mutans have greatly advanced our understanding of important areas in the field of bacteriology such as interspecies biofilms, competence development and stress responses. In this article, we provide an argument that places S. mutans, an organism that evolved in close association with the human host, as a novel Gram-positive model organism.Advances in the field of bacteriology have relied strongly on studies involving the bacterial paradigms Escherichia coli and Bacillus subtilis. In both cases, a long history of laboratory research, ease of cultivation and genetic manipulation encouraged and provided the rationale for the emergence of these bacteria as model organisms. E. coli is a Gramnegative, non-sporulating bacterium that can be found freeliving, in water or soil, as well as associated with plants, insects, birds and mammals. It is the most studied prokaryotic organism and comprises a very heterogeneous group containing both pathogenic and non-pathogenic strains. In addition to serving as the Gram-negative model organism, laboratory strains of E. coli are extremely versatile and are the quintessential lab workhorses. Bacillus subtilis is a Gram-positive sporulating organism commonly found in soil, plants and, transiently, on the surface of animals. Strains of B. subtilis are not associated with humans and are not pathogenic, although some closely related Bacillus species such as Bacillus anthracis and Bacillus cereus are implicated in human disease (anthrax) and in food poisoning, respectively. Because the sporulation process occurs in simple well-defined stages, B. subtilis sporulation has served as a paradigm for bacterial development and differentiation studies. Like E. coli, B. subtilis is also easy to cultivate and highly amenable to genetic manipulation. The wealth of information derived from investigations of the biochemistry, physiology, genetics and developmental processes of E. coli and B. subtilis laid the foundation for, and at the same time provided guidance for, studies with other bacterial species. In addition to E. coli and B. subtilis, there are numerous other organisms that have served, in a more limited scope, a...

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“…On the other hand their C-terminally located conserved domains TGS (this domain is conserved in threonyl t-RNA synthetase, GTPases and SpoT proteins) and ACT (this domain is conserved in acetolactate synthase, chorismate mutase and TyrR receptor proteins) (Aravind & Koonin, 1998;Atkinson et al, 2011;Potrykus & Cashel, 2008), are involved in regulation of enzymic activities (Battesti & Bouveret, 2006;Das et al, 2009;Gropp et al, 2001;Mechold et al, 2002;Schreiber et al, 1991). In SpoT/Rel enzymes, the hydrolase domain carries highly conserved histidine-aspartic acid (HD) residues (Aravind & Koonin, 1998;Das et al, 2009;Potrykus & Cashel, 2008). However, in RelA, the HD residues are substituted with other amino acids leading to impaired (p)ppGpp hydrolase activity function (Aravind & Koonin, 1998).…”

Section: Introductionmentioning

confidence: 99%

Genetic and mutational characterization of the small alarmone synthetase gene relV of Vibrio cholerae

et al. 2014

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In Vibrio cholerae, the causative agent of cholera, products of three genes, relA, spoT and relV, govern nutritional stress related stringent response (SR). SR in bacteria is critically regulated by two intracellular small molecules, guanosine 39-diphosphate 59-triphosphate (pppGpp) and guanosine 39,59-bis(diphosphate) (ppGpp), collectively called (p)ppGpp or alarmone. Evolution of relV is unique in V. cholerae because other Gram-negative bacteria carry only relA and spoT genes. Recent reports suggest that RelV is needed for pathogenesis. RelV carries a single (p)ppGpp synthetase or RelA-SpoT domain (SYNTH/RSD) and belongs to the small alarmone synthetase (SAS) family of proteins. Here, we report extensive functional characterizations of the relV gene by constructing several deletion and site-directed mutants followed by their controlled expression in (p)ppGpp 0 cells of Escherichia coli or V. cholerae. Substitution analysis indicated that the amino acid residues K107, D129, R132, L150 and E188 of the RSD region of RelV are essential for its activity. While K107, D129 and E188 are highly conserved in RelA and SAS proteins, L150 appears to be conserved in the latter group of enzymes, and the R132 residue was found to be unique in RelV. Extensive progressive deletion analysis indicated that the amino acid residues at positions 59 and 248 of the RelV protein are the functional N-and C-terminal boundaries, respectively. Since the minimal functional length of RelV was found to be 189 aa, which includes the 94 aa long RSD region, it seems that the flanking residues of the RSD are also important for maintaining the (p)ppGpp synthetase activity.

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Stringent response in Vibrio cholerae: genetic analysis of spoT gene function and identification of a novel (p)ppGpp synthetase gene

Cited by 71 publications

References 41 publications

Cholera Toxin Production during Anaerobic Trimethylamine N-Oxide Respiration Is Mediated by Stringent Response in Vibrio cholerae

Cholera Toxin Production during Anaerobic Trimethylamine N-Oxide Respiration Is Mediated by Stringent Response in Vibrio cholerae

Streptococcus mutans: a new Gram-positive paradigm?

Genetic and mutational characterization of the small alarmone synthetase gene relV of Vibrio cholerae

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