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PubMed1963

ACCUMULATION OF INORGANIC POLYPHOSPHATE IN AEROBACTER AEROGENES. I. RELATIONSHIP TO GROWTH AND NUCLEIC ACID SYNTHESIS.

Harold, F. M. (National Jewish Hospital, Denver, Colo.). Accumulation of inorganic polyphosphate in Aerobacter aerogenes. I. Relationship to growth and nucleic acid synthesis. J. Bacteriol. 86:216-221. 1963.-Growing cells of Aerobacter aerogenes contain traces of inorganic polyphosphate, but large amounts often accumulate when growth ceases as the result of a nutritional deficiency. The reciprocal relationship between growth and polyphosphate accumulation was traced to competition between nucleic acid synthesis and polyphosphate for intracellular phosphorus. Polyphosphate accumulated only after nucleic acid synthesis had ceased. Resumption of nucleic acid synthesis (with or without concurrent cell growth) induced rapid degradation of the polyphosphate with transfer of the phosphorus to ribonucleic acid (RNA). At the same time, incorporation of P(32) into polyphosphate was reduced, though not abolished. Competition for adenosine triphosphate may be part of the explanation. In addition, it appears that polyphosphate degradation is accelerated under conditions which permit rapid nucleic acid synthesis, the phosphorus released being trapped in RNA.

DNA↗

PubMed1998

Inorganic polyphosphate in human osteoblast-like cells.

Significant amounts of inorganic polyphosphates and of polyphosphate-degrading exopolyphosphatase activity were detected in human mandibular-derived osteoblast-like cells. The amount of both soluble and insoluble long-chain polyphosphate in unstimulated osteoblast-like cells was higher than in human gingival cells, erythrocytes, peripheral blood mononuclear cells, and human blood plasma. The cellular content of polyphosphate in osteoblast-like cells strongly decreased after a combined treatment of the cells with the stimulators of osteoblast proliferation and differentiation, dexamethasone, beta-glycerophosphate, epidermal growth factor, and ascorbic acid. The amount of soluble long-chain polyphosphate, but not the amount of insoluble long-chain polyphosphate, further decreased after an additional treatment with 1alpha,25-dihydroxyvitamin D3 (1,25(OH)2D3). The decrease in polyphosphate content during treatment with dexamethasone, beta-glycerophosphate, epidermal growth factor, and ascorbic acid was accompanied by a decrease in exopolyphosphatase, pyrophosphatase, and alkaline phosphatase activity. However, additional treatment with 1,25(OH)2D3 resulted in an increase in these enzyme activities. Osteoblast-like cell exopolyphosphatase activity and exopolyphosphatase activity in yeast, rat tissues, and human leukemia cell line HL60 were inhibited by the bisphosphonates etidronate and, to a lesser extent, clodronate and pamidronate. From our results, we assume that inorganic polyphosphate may be involved in modulation of the mineralization process in bone tissue.

Acid Anhydride Hydrolases↗

PubMed1998

Optimization of polyphosphate degradation and phosphate secretion using hybrid metabolic pathways and engineered host strains

Polyphosphate degradation and phosphate secretion were optimized in Escherichia coli strains overexpressing the E. coli polyphosphate kinase gene (ppk) and either the E. coli polyphosphatase gene (ppx) or the Saccharomyces cerevisiae polyphosphatase gene (scPPX1) from different inducible promoters on medium- and high-copy plasmids. The use of a host strain without functional ppk or ppx genes on the chromosome yielded the highest levels of polyphosphate, as well as the fastest degradation of polyphosphate when the gene for polyphosphatase was induced. The introduction of a hybrid metabolic pathway consisting of the E. coli ppk gene and the S. cerevisiae polyphosphatase gene resulted in lower polyphosphate concentrations than when using both the ppk and ppx genes from E. coli, and did not significantly improve the degradation rate. It was also found that the rate of polyphosphate degradation was highest when ppx was induced late in growth, most likely due to the high intracellular polyphosphate concentration. The phosphate released from polyphosphate allowed the growth of phosphate-starved cells; excess phosphate was secreted into the medium, leading to a down-regulation of the phosphate-starvation (Pho) response. The production of alkaline phosphatase, an indicator of the Pho response, can be precisely controlled by manipulating the degree of ppx induction. Copyright 1998 John Wiley & Sons, Inc.

Journal Article↗

PubMed1995

Alterations of inositol polyphosphates in skeletal muscle during porcine malignant hyperthermia.

Malignant hyperthermia (MH) may result from increased intracellular calcium concentrations. Increased 1,4,5-IP3 concentrations could mediate this increase in Ca2+. In this study we measured inositol polyphosphates in selectively bred MH susceptible (MHS) and MH non-susceptible (MHN) swine. MH crisis was induced by halothane challenge, and dantrolene was administered in order to measure inositol polyphosphates after MH reversal. Muscle biopsies of skeletal muscles of the hind limbs were obtained in random order and inositol polyphosphates determined by high pressure liquid chromatography using a metal dye detection method. Inositol polyphosphates were determined in three groups: (1) MHS vs MHN basal, (2) during MH crisis induced by halothane and (3) following treatment with dantrolene after halothane challenge. Clinical variables (P(_)VO2, P(-)VCO2, PE'CO2 and pH) indicated that MH was readily induced in MHS swine. Basal concentrations of all inositol polyphosphates were higher in MHS swine compared with MHN swine. After halothane challenge, 1,3,4-IP3, 1,3,4,6-IP4 and 1,3,4,5-IP4 concentrations increased in MHS animals compared with the respective baseline values, whereas no changes in MHN animals could be detected. Dantrolene administration decreased inositol polyphosphate concentrations in MHS swine. MHN swine showed no changes in inositol polyphosphates after dantrolene. These findings indicate that inositol polyphosphates may be involved in metabolic changes after triggering and treatment of MH.

Anesthetics, Inhalation↗

PubMed1988

A kinetic study of the inhibition of yeast AMP deaminase by polyphosphate.

Inorganic pyrophosphate and polyphosphates have acted as potent inhibitors of purified AMP deaminase (EC 3.5.4.6) from yeast: the activity fell to a definite limit with the increase in the concentration of the inhibitor. The effect of polyphosphate was largely on the maximal velocity of the enzyme with some decrease in affinity. The cooperative effect of AMP, analyzed in terms of a Hill coefficient, remained at 2 in the absence and presence of polyphosphate. Binding of polyphosphate to the enzyme showed no cooperativity. The inhibition of AMP deaminase by polyphosphate can be qualitatively and quantitatively accounted for by the partial mixed-type inhibition mechanism. Both the Ki value for the inhibitor and the breakdown rate of the enzyme-substrate-inhibitor complex are dependent on the chain length of polyphosphate, suggesting that the breakdown rate of the enzyme-substrate-inhibitor complex is regulated by binding of polyphosphate to a specific inhibitory site.

AMP Deaminase↗

PubMed1989

Polyphosphate synthesis in yeast.

Polyphosphate synthesis was studied in phosphate-starved cells of Saccharomyces cerevisiae and Kluyveromyces marxianus. Incubation of these yeasts for a short time with phosphate and either glucose or ethanol resulted in the formation of polyphosphate with a short chain length. With increasing incubation times, polyphosphates with longer chain lengths were formed. Polyphosphates were synthesized faster during incubation with glucose than with ethanol. Antimycin did not affect the glucose-induced polyphosphate synthesis in either yeast. Using ethanol as an energy source, antimycin A treatment blocked both polyphosphate synthesis and accumulation of orthophosphate in the yeast S. cerevisiae. However, in K. marxianus, polyphosphate synthesis and orthophosphate accumulation proceeded normally in antimycin-treated cells, suggesting that endogenous reserves were used as energy source. This was confirmed in experiments, conducted in the absence of an exogenous energy source.

Adenosine Triphosphate↗

PubMed1993

Effects of osmotic stress and growth stage on cellular pH and polyphosphate metabolism in Neurospora crassa as studied by 31P nuclear magnetic resonance spectroscopy.

High-resolution 31P-NMR was employed to investigate the effects of growth stage and environmental osmolarity on changes of polyphosphate metabolism and intracellular pH in intact Neurospora crassa cells. Our study showed that changes of these parameters were growth-dependent. The ratio of polyphosphate to orthophosphate in vacuoles increased from 2.4 to 13.5 in N. crassa as cells grew from early log phase to stationary phase. Cytoplasmic pH and vacuolar pH changed, respectively, from 6.91 and 6.49 in early log phase cells to 7.25 and 6.84 in stationary phase cells. Hypoosmotic shock of N. crassa produced growth-dependent changes including: (i) a rapid hydrolysis of polyphosphate with a concomitant increase in the concentration of the cytoplasmic phosphate, (ii) an increase in cytoplasmic pH, and (iii) an increase in vacuolar pH. Early log phase cells produced the most dramatic response whereas the stationary phase cells appeared to be recalcitrant to the osmotic stress. Thus, 95% and 60% of polyphosphate in the early log phase and mid-log phase cells, respectively, disappeared in response to hypoosmotic shock, but little or no hydrolysis of polyphosphate occurred in stationary cells. The cytoplasmic pH and the vacuolar pH increased in response to hypoosmotic shock by 0.4 and 0.53 unit, respectively, in early log phase cells; and by 0.22 and 0.27 unit, respectively, in the mid-log phase cells. In contrast, hypoosmotic shock of the stationary phase cells did not cause any change in intracellular pH. The osmotic stress-induced polyphosphate hydrolysis and pH changes in early log and mid-log phase cells were reversible, suggesting that these changes were related environment osmolarity. Addition of polyamines or basic amino acids which are known to be sequestered in vacuoles did not effect polyphosphate metabolism.

Amino Acids↗

PubMed2000

Effect of electrical stimulation and polyphosphate marination on drip from early-harvested, individually quick-frozen chicken breast fillets.

Individual and combined effects of electrical stimulation and polyphosphate marination on drip and other quality attributes of early-harvested, individually quick-frozen chicken breast fillets were evaluated. Broiler chickens were slaughtered, half conventionally processed and half with electrical stimulation. Fillets were harvested 1 h postmortem and marinated in either NaCl solution or NaCl plus polyphosphate solution. Marinade absorption, pH, drip, cooking loss, and shear values were observed. Electrical stimulation had no direct effect on pH, cooking loss, or shear values, whereas polyphosphate increased pH and decreased cooking loss. Polyphosphate treatment caused fillets from unstimulated carcasses to absorb more marinade and yielded more drip that those from stimulated carcasses. Fillets from stimulated carcasses marinated in NaCl solution without polyphosphate yielded less drip than those from unstimulated carcasses. Polyphosphate reduced drip of fillets from unstimulated carcasses but not of those from stimulated carcasses. Results support previous reports indicating interactions between polyphosphates and processing parameters that can affect ultimate quality of poultry meat products.

Animals↗

PubMed2002

Polyphosphate produced in recombinant Escherichia coli confers mercury resistance.

An Escherichia coli strain was generated by fusion of a merA-deleted broad-spectrum mer operon from Pseudomonas K-62 with a bacterial polyphosphate kinase gene (ppk) from Klebsiella aerogenes in vector pUC119. A large amount of the ppk-specified polyphosphate was identified in the mercury-induced bacterium with the fusion plasmid designated pMKB18 but not in the cells without mercury induction. These results suggest that the synthesis of polyphosphate as well as the expression of the mer genes is mercury-inducible and regulated by merR. The E. coli strain with pMKB18 was more resistant to both Hg2+ and C6H5Hg+ than its isogenic strain with cloning vector pUC119. The recombinant strain accumulated more mercury from Hg2+- and C6H5Hg+-contaminated medium. Hg2+ transported into the cytoplasm appeared to be bound by chelation with the polyphosphate produced by the recombinant cells. The transported phenylmercury was degraded to Hg2+ before the chelation since polyphosphate did not directly chelate with C6H5Hg+. These results indicate that polyphosphate is capable of reducing the cytotoxicity of the transported Hg2+ probably via chelation between polyphosphate and Hg2+.

Drug Resistance↗

PubMed1989

Polyphosphate-degrading enzymes in Acinetobacter spp. and activated sludge.

Polyphosphate-degrading enzymes were studied in Acinetobacter spp. and activated sludge. Polyphosphate: AMP phosphotransferase activity in Acinetobacter strain 210A decreased with increasing growth rates. The activity of this enzyme in cell extracts of Acinetobacter strain 210A was maximal at a pH of 8.5 and a temperature of 40 degrees C and was stimulated by (NH4)2SO4. The Km for AMP was 0.6 mM, and the Vmax was 60 nmol/min per mg of protein. Cell extracts of this strain also contained polyphosphatase, which was able to degrade native polyphosphate and synthetic magnesium polyphosphate and was strongly stimulated by 300 to 400 mM NH4Cl. A positive correlation was found between polyphosphate:AMP phosphotransferase activity, adenylate kinase activity, and phosphorus accumulation in six Acinetobacter strains. Significant activities of polyphosphate kinase were detected only in strain P, which contained no polyphosphate:AMP phosphotransferase. In samples of activated sludge from different plants, the activity of adenylate kinase correlated well with the ability of the sludge to remove phosphate biologically from wastewater.

Acid Anhydride Hydrolases↗

PubMed1977

[Polyphosphate kinase activity in yeast vacuoles].

The enzyme polyphosphate kinase (ATP: Polyphosphate phosphotransferase EC 2.7.4.1) relating to the class of transferases was detected in the vacuoles of Saccharomyces carlsbergensis yeast. The direct ATP: Polyphosphate phosphotransferase reaction resulting in the synthesis of polyphosphates from ATP was shown to occur mainly in vacuoles. The localization of the reverse polyphosphate: ADP phosphatransferase reaction was not established in any of the subcellular yeast fractions studied. The activity of the direct reaction in the yeast protoplasts makes up about 1% of the reverse one, but in vacuoles it is significantly higher and makes up to 19%. Under activation of biochemical processes involved in the production of cell wall components by protoplasts, vacuolar polyphosphates work mainly in the direction of ATP synthesis at the expense of polyphosphates accumulated in vacuoles.

Adenosine Triphosphate↗

PubMed1981

[Interrelationship of polyphosphate metabolism and levorin biosynthesis in Streptomyces levoris].

The effect of inorganic phosphate on biosynthesis of the polyene antibiotic levorin by Streptomyces levoris was studied. At phosphate concentration of 4.0 mM levorin biosynthesis is repressed by 90%, resulting in an increase of ATP and a condensed inorganic polyphosphates content in the producer cells. At phosphate concentration optimal for levorin production (0.04 mM) the level of intracellular ATP sharply falls by the beginning of the steady-state phase of the producer growth and that of polyphosphates decreases 3-6-fold. The inorganic phosphate exerts different effects on polyphosphate metabolism enzymes, such as polyphosphate: D-glucose-6-phosphotransferase, polyphosphate phosphohydrolase, tripolyphosphate phosphohydrolase, pyrophosphate phosphohydrolase, alkaline and acid phosphatase. The strongest effect of phosphate excess is observed in the case of polyphosphate: D-glucose-6-phosphotransferase, whose activity decreases 2-5-fold. The activity of this enzyme was shown to be correlated with the antibiotic accumulation. The data obtained are indicative of interrelationship between the polyphosphate metabolism and levorin biosynthesis.

Adenosine Triphosphate↗

PubMed1995

A novel receptor for diadenosine polyphosphates coupled to calcium increase in rat midbrain synaptosomes.

1. Diadenosine polyphosphates, Ap4A and Ap5A, as well as ATP, alpha,beta-MeATP and ADP-beta-S, were able to elicit variable intrasynaptosomal Ca2+ increases in rat midbrain synaptic terminals. The origin of the Ca2+ increment was the extra synaptosomal space since the elimination of extracellular Ca2+ abolished the effect of all the agonists. 2. The P2-purinoceptor antagonist, suramin, did not affect the Ca(2+)-increase evoked by diadenosine polyphosphates but dramatically blocked the Ca2+ entry induced by ATP and its synthetic analogues. 3. The actions of Ap5A and ATP on the intrasynaptosomal Ca2+ increase did not cross-desensitize. 4. Concentration-response studies for diadenosine polyphosphates showed pD2 values of 54.5 +/- 4.2 microM and 55.6 +/- 3.8 microM for Ap4A and Ap5A, respectively. 5. The entry of calcium induced by diadenosine polyphosphates could be separated into two components. The first represented a selective voltage-independent Ca2+ entry; the second, a sustained phase which was voltage-dependent. 6. Studies on the voltage-dependent Ca(2+)-channels involved in the effects of the diadenosine polyphosphates, demonstrated that omega-conotoxin G-VI-A inhibited the sustained Ca(2+)-entry, suggesting the participation of an N-type Ca(2+)-channel. This toxin was unable to abolish the initial cation entry induced by Ap4A or Ap5A. omega-Agatoxin IV-A, tetrodotoxin, or nifedipine did not inhibit the effects of the diadenosine polyphosphates. 7. The effect of ATP on Ca(2+)-entry was abolished by nifedipine and omega-conotoxin G-VI-A, suggesting the participation of L- and N-type Ca(2+)-channels in the response to ATP. 8. These data suggest that Ap4A, Ap5A and ATP activate the same intracellular Ca2+ signal through different receptors and different mechanisms. Ap4A and Ap5A induce a more selective Ca2+-entry in a voltage-independent process. This is the first time that a selective action of diadenosine polyphosphate through receptors other than P1 and P2-purinoceptors has been described.

Adenosine Triphosphate↗

PubMed1970

Polyphosphate and orthophosphate content of Nitrosomonas europaea as a function of growth.

After inoculation of a stationary-phase culture of Nitrosomonas europaea into fresh growth solution, the cell-associated orthophosphate increased rapidly to 800 mumoles/g (wet weight), whereas the acid-insoluble long-chain polyphosphate content decreased rapidly to 22 mumoles/g. As growth proceeded, the orthophosphate content decreased rapidly to a level of 15 mumoles/g and the long-chain polyphosphate content gradually increased to 60 to 90 mumoles/g. When the pH of a culture of Nitrosomonas decreased during growth below approximately 7.4, the rate of nitrite and polyphosphate synthesis increased and the ratio of change in protein to change in nitrite decreased. When the pH of the culture was maintained above 7.6 throughout growth, polyphosphate accumulation, an increased rate of nitrite and polyphosphate synthesis, and a decreased ratio of change in protein to change in nitrite were not observed. Cells of Nitrosomonas apparently accumulated polyphosphate when adenosine triphosphate generated during the oxidation of ammonia to nitrite was not efficiently used to promote an increase in cell mass. The rapid hydrolysis of polyphosphate after the transfer of stationary-phase cells into fresh growth solution was found to be triggered primarily by the higher pH of the fresh growth solution. The efflux of orthophosphate during culture growth was not associated with a decrease in the pH of the growth solution. Data on the chemical composition of Nitrosomonas are presented.

Adenosine Triphosphate↗

PubMedDate not supplied

Engineering polyphosphate metabolism in Escherichia coli: implications for bioremediation of inorganic contaminants.

Polyphosphate metabolism plays an important role in the bioremediation of phosphate contamination in municipal wastewater, and may play a key role in heavy metal tolerance and bioremediation. However, little is known about the regulation of polyphosphate metabolism in microorganisms and its role in heavy metal toxicity. We have manipulated polyphosphate metabolism in Escherichia coli by overexpressing the genes for polyphosphate kinase (ppk) and for polyphosphatase (ppx) under control of their native promoters and inducible promoters. Overexpression of ppk results in high levels of intracellular polyphosphate, improved phosphate uptake, but no increase in tolerance to heavy metals. Overexpression of both ppk and ppx results in lower levels of intracellular polyphosphate, secretion of phosphate from the cell, and increased tolerance to heavy metals. Metabolic flux analysis indicates that the cell responds to increased flux through the PPK-PPX pathway by altering flux through the TCA cycle.

Acid Anhydride Hydrolases↗

PubMed1990

Determination of the role of polyphosphate in transport-coupled phosphorylation in the yeast Saccharomyces cerevisiae.

The role of polyphosphate in 2-deoxy-D-glucose transport was studied in yeast cells, pulse-labeled with [32P]orthophosphate, by comparing the concentrations and specific activities of polyphosphate, orthophosphate and 2-dGlc-phosphate. When 2-dGlc transport was measured under aerobic conditions, it appeared that polyphosphate replenished the orthophosphate pool, indicating that polyphosphate has, at least mainly, an indirect role in sugar phosphorylation. Also in cells with a reduced respiratory capacity, due to a treatment with antimycin A, no direct role for polyphosphate in 2-dGlc transport could be detected. Under these conditions, only a very limited breakdown of polyphosphate occurred, probably because of the small decrease in the orthophosphate concentration.

Antimycin A↗

PubMed2002

Enhanced phosphate uptake and polyphosphate accumulation in Burkholderia cepacia grown under low pH conditions.

Of bacterial cells in a sample of activated sludge, 34% contained detectable intracellular polyphosphate inclusions following Neisser staining, when grown on glucose/mineral salts medium at pH 5.5; at pH 7.5 only 7% of cells visibly accumulated polyphosphate. In a sludge isolate of Burkholderia cepacia chosen for further study, maximal removal of phosphate and accumulation of polyphosphate occurred at pH 5.5; levels were up to 220% and 330% higher, respectively, than in cells grown at pH 7.5. During the early stationary phase of growth at pH 5.5 a maximum level of intracellular polyphosphate that comprised 13.6% of cellular dry weight was reached. Polyphosphate kinase activity was detected in actively growing cells only when cultured at pH 5.5. The phenomenon of acid-stimulated phosphate uptake and polyphosphate accumulation in this environmental bacterial population parallels observations previously made by us in the yeast Candida humicola and may thus represent a widespread microbial response to low external pH values.

Burkholderia cepacia↗

PubMed1995

Effect of polyphosphates on the activity of amine oxidases.

The interaction between polyphosphates and polyamines was investigated by 31P-NMR spectroscopy and by amine oxidase activity measurements. An apparent competition between negatively charged polyphosphates (ATP, ADP, AMP, tripolyphosphate and pyrophosphate) and positively charged polyamine, for the active site of bovine serum and soybean seedling amine oxidases, was observed by activity measurements. This behavior was explained by formation of polyamine-polyphosphate complexes and the stability constants of these complexes were calculated by 31P NMR. However, at a given concentration of polyphosphate, the amine oxidase activity was found higher than that expected on the basis of the free amine concentration calculated according to the NMR stability constant. This fact, and the different extent of inhibition of the spermidine oxidase activity of soybean seedling and of bovine serum amine oxidases observed in the presence of a given polyphosphate, suggest that amine oxidases may be active also on the polyamine-polyphosphate complexes. This hypothesis was supported by the strong dependence of the kcat/Km of bovine serum amine oxidase on ionic strength, indicating an electrostatic interaction between the charged amine and the active site, while no effect of ionic strength on kcat/Km was observed in the presence of ATP. A kinetic model of this behavior was found to fit the experimental data.

Amine Oxidase (Copper-Containing)↗