Pyrophosphatase is essential for growth of Escherichia coli

@article{Chen1990PyrophosphataseIE,
  title={Pyrophosphatase is essential for growth of Escherichia coli},
  author={J. Chen and A. Brevet and M. Fromant and F. Leveque and J. Schmitter and S. Blanquet and P. Plateau},
  journal={Journal of Bacteriology},
  year={1990},
  volume={172},
  pages={5686 - 5689}
}
The ppa gene for inorganic pyrophosphatase is essential for the growth of Escherichia coli. A recombinant with a chromosomal ppa::Kanr lesion and a temperature-sensitive replicon with a ppa+ gene showed a temperature-sensitive growth phenotype, and a mutant with the sole ppa+ gene under control of the lac promoter showed inducer-dependent growth. When the lacp-ppa mutant was subcultured without inducer, the pyrophosphatase level decreased, the PPi level increased, and growth stopped. Cellular… Expand
In vivo positive effects of exogenous pyrophosphate on Escherichia coli cell growth and stationary phase survival.
We have studied the effect of exogenous pyrophosphate on growing cells of Escherichia coli. In the presence of 10 mM of pyrophosphate, the entry into the stationary phase was delayed and thus aExpand
Rhodospirillum rubrum has a family I pyrophosphatase: purification, cloning, and sequencing
TLDR
The cytoplasmic pyrophosphatase of the photosynthetic bacterium Rhodospirillum rubrum was purified to electrophoretic homogeneity and alignment of the deduced 179-amino-acid protein with known bacterial pyroph phosphatases revealed conservation of all residues in the active site. Expand
Cloning and expression of the inorganic pyrophosphatase gene from the amino acid producer Brevibacterium lactofermentum ATCC 13869.
TLDR
The cloned ppa gene was cloned from B. lactofermentum chromosomal DNA by polymerase chain reaction; it seemed to be an essential gene and it might represent an attractive target for drug discovery. Expand
Inhibition of Escherichia coli inorganic pyrophosphatase by fructose-1-phosphate
TLDR
Fru-1-P is a physiological inhibitor of pyrophosphatase that acts via a regulatory site in this enzyme, and is demonstrated to be a mechanism not involving competition with substrate for binding to the active site. Expand
Cloning and expression of a unique inorganic pyrophosphatase from Bacillus subtilis: evidence for a new family of enzymes
An open reading frame located in the COTF‐TETB intergenic region of Bacillus subtilis was cloned and expressed in Escherichia coli and shown to encode inorganic pyrophosphatase (PPase). The isolatedExpand
Expression in Escherichia coli of the thermostable inorganic pyrophosphatase from the Aquifex aeolicus and purification and characterization of the recombinant enzyme.
TLDR
The gene encoding the inorganic pyrophosphatase from a hyperthermophilic bacterium, Aquifex aeolicus (Aae), was amplified by PCR and overexpressed in Escherichia coli using a pJR-based expression plasmid, pAIPD, and showed the optimal activity in the pH range 7.5-8.0. Expand
Some properties of inorganic pyrophosphatase from Bacillus subtilis.
Inorganic pyrophosphatase (pyrophosphate phosphohydrolase, EC 3.6.1.1; PPase) from Bacillus subtilis was purified to a homogeneous state electrophoretically when analysed by SDS-PAGE. The enzymeExpand
Identification of an Arabidopsis inorganic pyrophosphatase capable of being imported into chloroplasts
An Arabidopsis cDNA coding for a previously uncharacterized isoform of inorganic pyrophosphatase was isolated. It was used to complement an E. coli mutant, demonstrating that it coded for an activeExpand
Cloning, functional expression, and complementation analysis of an inorganic pyrophosphatase from Bartonella bacilliformis.
TLDR
The cloned inorganic pyrophosphatase gene (ppa) from the facultative intracellular pathogen Bartonella bacilliformis is cloned and its encoded product is characterized, which is in agreement with in vitro and in vivo synthesis of a protein with an apparent molecular mass of 22-23 kDa. Expand
Characterization of the 5' flanking region of the Escherichia coli ppa gene encoding inorganic pyrophosphatase: mutations in the ribosome-binding site decrease the level of ppa mRNA.
TLDR
When the -35 sequence of ppa, AAGACA, was mutated to AAAACA, ppa expression, as measured by PPase production, decreased to 20% of the wild-type, whereas by the change of the -10 sequence, TATAAT, to TTTAAT or TATAAA, the ppa gene was totally inactivated and the intracellular levels of both ppa mRNA and PPase decreased drastically. Expand
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References

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Intracellular PPi concentration is not directly dependent on amount of inorganic pyrophosphatase in Escherichia coli K-12 cells
TLDR
No correlation was observed between the level of inorganic pyrophosphatase (PPase) and the intracellular concentration of PPi in Escherichia coli cells, and the PPi concentration could, however, be increased or decreased from the control level under some stressful conditions. Expand
Fructose bisphosphatase of Escherichia coli: cloning of the structural gene (fbp) and preparation of a chromosomal deletion
TLDR
In vivo mutagenesis of the clone was used to show that fbp is the structural gene, and the chromosomal wild-type locus was replaced with this deletion by a method involving stabilization of a heterozygous intermediate resulting from plasmid integration, followed by segregation of the wild- type gene. Expand
Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12
TLDR
The Escherichia coli K-12 gene ppa encoding inorganic pyrophosphatase (PPase) was cloned and sequenced, the first report of the cloning of a PPase gene. Expand
The intracellular concentration of pyrophosphate in the batch culture of Escherichia coli.
TLDR
The intracellular concentration of PPi in the batch culture of Escherichia coli was about 2.5 nmol PPi/mg protein (0.5 mM) and a similar concentration was found in cells growing in minimal medium enriched by amino acid mixture. Expand
Regulation of Intracellular Pyrophosphatase-Activity and Conservation of the Phosphoanhydride-Energy of Inorganic Pyrophosphate in Microbial Metabolism
  • J. Klemme
  • Chemistry, Medicine
  • Zeitschrift fur Naturforschung. Section C, Biosciences
  • 1976
TLDR
The rate of intracellular PP-liberation during biosynthesis of cellular constituents is calculated from the specific growth rate and the macromolecular composition of the respective microorganism to investigate the possibility of the limitation of biosynthesis through PPase-activity. Expand
Genetic engineering of methionyl-tRNA synthetase: in vitro regeneration of an active synthetase by proteolytic cleavage of a methionyl-tRNA synthetase--beta-galactosidase chimeric protein.
The construction of a family of plasmids carrying derivatives of metG, the gene for E. coli methionyl-tRNA synthetase, is described. These plasmids allow expression of native or truncated forms ofExpand
Construction of an Hfr strain useful for transferring recA mutations between Escherichia coli strains
TLDR
Strain JC10240 (Hfr PO45 srlC300::Tn10 recA56 thr-300 ilv-318 rpsE300) was constructed and can be moved to other Escherichia coli strains in transductional or conjugational crosses selecting resistance to tetracycline. Expand
Molecular cloning of the Escherichia coli gene for diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase
TLDR
It was shown that the overproduction of diadenosine tetraph phosphatase decreased the dinucleoside tetraphosphate concentration in E. coli by a factor of 10. Expand
The mechanism of action of yeast inorganic pyrophosphatase.
TLDR
This chapter reviews the current status of the knowledge of PPase, and briefly discusses experiments in progress which should extend this knowledge, and formulation of a model for the catalytic mechanism that includes two factors known to be important for raising the rates of nonenzymatic phosphoryl transfer. Expand
New method for generating deletions and gene replacements in Escherichia coli
TLDR
A method for generating gene replacements and deletions in Escherichia coli using a temperature-sensitive pSC101 replicon to facilitate the gene replacement and can be used to generate deletions of essential genes. Expand
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