Isolation of a pyrophosphorylase from <i>Bacillus subtilis</i> and <i>Bacillus stearothermophilus</i> that specifically degrades guanosine 3′‐diphosphate 5′‐diphosphate

Richter, Dietmar; Geis, Monika

doi:10.1016/0014-5793(78)80411-6

Cited by 8 publications

(5 citation statements)

References 13 publications

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“…The spoT gene product in E. coli plays a role in the degradation of guanosine 3'-diphosphate 5'-di-and triphosphate (the "magic spots"; 1,8,9,18). Our data suggest that this same gene product may be responsible for the degradation of cyclic GMP in addition, although we do not know whether the transient accumulation that we observe results from increased synthesis or decreased degradation.…”

mentioning

confidence: 66%

Is cyclic guanosine 3',5'-monophosphate a cell cycle regulator?

Cook¹,

Kalb²,

Peace³

et al. 1980

J Bacteriol

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mentioning

confidence: 66%

Is cyclic guanosine 3',5'-monophosphate a cell cycle regulator?

Cook¹,

Kalb²,

Peace³

et al. 1980

J Bacteriol

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“…This is abolished in the disruption mutants, as is also the case for S. coelicolor and B. subtilis. Analysis of the stability of (p)ppGpp in B. subtilis wild type and the relaxed mutant BR17 suggested the existence of a spoT gene (Richter and Geis, 1978;Belitsky and Shakulov, 1982), although residual synthesizing and degrading activities of the mutant RelA protein had not been measured in vitro. Given the high sequence similarity of the relA gene from B. subtilis to rel S. equisimilis , and the physiological features of BR17 and our deletion mutant TW30, we propose that the B. subtilis relA gene substitutes for both relA and spoT genes of E. coli.…”

Section: Discussionmentioning

confidence: 99%

Cloning and characterization of a relA/spoT homologue from Bacillus subtilis

Wendrich

Marahiel

1997

Molecular Microbiology

148

131

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SummaryA PCR-amplified DNA fragment of the relA gene from genomic Bacillus subtilis DNA was used to isolate the entire relA /spoT homologue and two adjacent open reading frames (ORFs) from a ZAP Express library. The relA gene, which encodes a protein of 734 amino acid residues (aa), is flanked by an ORF (170 aa) that shares high similarity to adenine phosphoribosyltransferase genes (apt), and downstream by an ORF (131 aa) of unknown function. This genetic organization is similar to that in Streptomyces coelicolor A3(2) and Streptococcus equismilis H46A. relA shows significant similarity to the Escherichia coli relA and spoT genes, which are responsible for the synthesis and degradation of the highly phosphorylated guanosine nucleotides (p)ppGpp, triggering the stringent response. Deletion of the relA gene generated a (p)ppGpp 0 phenotype that demonstrated its essential role in the response to amino acid deprivation and resulted in impaired/ lowered induction of proteins involved in stress response as well as amino acid biosynthesis, as judged by two-dimensional gel electrophoresis. The same effects of impaired induction of some B -independent proteins could also be shown in a sigB/relA double mutant, supporting the role of relA in derepression/ induction of catabolic and anabolic genes during stringent response.

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“…This activity, responsible for the splitting of ppGpp into GDP and very likely pyrophosphate was found associated with ribosomes, even in bacteria other than Escherichia coli [52]. Inhibitors of ribosome functions however were inactive on ppGpp degradation in vitro [37] and ribosomes themselves were not absolutely necessary for the reaction [52].…”

Section: Discussionmentioning

confidence: 99%

“…Inhibitors of ribosome functions however were inactive on ppGpp degradation in vitro [37] and ribosomes themselves were not absolutely necessary for the reaction [52].…”

Section: Discussionmentioning

confidence: 99%

The Energy‐Dependent Degradation of Guanosine 5′‐Diphosphate 3′‐Diphosphate in Escherichia coli

Tetu¹,

Dassa²,

Boquet³

1980

European Journal of Biochemistry

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Different inhibitors of the energy metabolism have been assayed in Escherichia coli K12 for their ability to increase the level of guanosine 5'-diphosphate 3'-diphosphate (ppGpp) as a consequence of a restriction of its degradation. Inhibitors of the respiration and uncouplers of oxidative phosphorylations had effects similar to carbon-source-induced downshifts while the ATPase inhibitor dicyclohexylcarbodiimide was less efficient. The effects of dicyclohexylcarbodiimide and of the uncoupler carbonylcyanide p-fluoro methoxyphenylhydrazone (FCCP) on ppGpp degradation were compared in a drug-permeable envelope mutant. At concentrations of inhibitors sufficient to deplete the pool of ATP by 50 %, only FCCP was able to block ppGpp degradation. Moreover, FCCP also inhibited ppGpp degradation in a ATPase-deficient strain growing on glucose as carbon source while, as expected, it did not change the level of ATP. It is concluded, according to Mitchell's chemiosmotic hypothesis, that, in vivo, the integrity of the transmembrane proton gradient rather than the ATP pool size is a prerequisite for the normal processing of the energy-dependent degradation of ppGpp.Numerous functions in the bacterial cell are presently known to be regulated by guanosine 5'-diphosphate 3'-diphosphate (ppGpp) (for review see [I]). This compound which was also reported in chloroplasts [2] and mitochondria [3] appears as a general metabolic effector in procaryotes. If on one hand, ppGpp inhibits the synthesis of what might be called the 'structural' material of the cell, such as ribosomal RNA [4-71, ribosomal proteins [8-301, lipids [ l l , 121, peptidoglycan [13] etc., on the other hand it stimulates the expression of some inducible operons [4,The intracellular level of ppGpp may itself be greatly modified as a function of nutrient availability and other growth conditions. The mechanism of the relA gene product-dependent synthesis of ppGpp observed in the course of amino acid starvations, which constitutes a very early event of the stringent response, is now well understood [17--251. All deficiencies in the charge of tRNA also lead to an elevated level of guanosine 5'-triphosphate 3'-diphosphate (pppGpp), the physiological precursor of ppGpp 14-161.Abbreviations. ppGpp, guanosine 5'-diphosphate 3'-diphosphate; pppGpp, guanosine 5'-triphosphate 3'-diphosphate; FCCP, carbonylcyanide-p-trifluoromethoxyphenylhydrazone; (cHxN)zC, dicyclohexylcarbodiimide.[26-281. An accumulation of the single ppGpp can be elicited by carbon-source substitutions [29,30] energy poisons [3 I] or membrane-perturbating agents such as morphine analogs [32,33], i.e. treatments which do not affect the incorporation of amino acids but create a defined situation of unbalanced growth (downshifts). All these conditions, which do not change the basal level of ppGpp synthesis, have been found to reduce considerably the rate of ppGpp degradation [29,32].Mutations in the spoT gene were shown to have a similar effect [34,35] and recent experiments of ppGpp degradation in vitro ha...

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Isolation of a pyrophosphorylase from Bacillus subtilis and Bacillus stearothermophilus that specifically degrades guanosine 3′‐diphosphate 5′‐diphosphate

Cited by 8 publications

References 13 publications

Is cyclic guanosine 3',5'-monophosphate a cell cycle regulator?

Is cyclic guanosine 3',5'-monophosphate a cell cycle regulator?

Cloning and characterization of a relA/spoT homologue from Bacillus subtilis

The Energy‐Dependent Degradation of Guanosine 5′‐Diphosphate 3′‐Diphosphate in Escherichia coli

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