Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Membrane-bound pyrophosphatase of the hyperthermophilic bacterium Thermotoga maritima(Tm-PPase), a homologue of H(+)-translocating pyrophosphatase, was expressed in Escherichia coli and isolated as inner membrane vesicles. In contrast to all previously studied H(+)-PPases, both native and recombinant Tm-PPases exhibited an absolute requirement for Na(+) but displayed the highest activity in the presence of millimolar levels of both Na(+) and K(+). Detergent-solubilized recombinant Tm-PPase was thermostable and retained the monovalent cation requirements of the membrane-embedded enzyme. Steady-state kinetic analysis of pyrophosphate hydrolysis by the wild-type enzyme suggested that two Na(+) binding sites and one K(+) binding site are involved in enzyme activation. The affinity of the site that binds Na(+) first is increased with increasing K(+) concentration. In contrast, only one Na(+) binding site (K(+)-dependent) and one K(+) binding site were involved in activation of the Asp(703) --> Asn variant. Thus, Asp(703) may form part of the K(+)-independent Na(+) binding site. Unlike all other membrane and soluble PPases, Tm-PPase did not catalyze oxygen exchange between phosphate and water. However, solubilized Tm-PPase exhibited low but measurable PP(i)-synthesizing activity, which also required Na(+) but was inhibited by K(+). These results demonstrate that T. maritima PPase belongs to a previously unknown subfamily of Na(+)-dependent H(+)-PPase homologues and may be an analogue of Na(+),K(+)-ATPase.
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PMID:Membrane-bound pyrophosphatase of Thermotoga maritima requires sodium for activity. 1569 34

Sodium at high millimolar levels in the cytoplasm is toxic to plant and yeast cells. Sequestration of Na+ ions into the vacuole through the action of tonoplast proton pumps (an H+ -ATPase in the case of yeast, and either a H+ -pyrophosphatase (H+ -PPase) or H+ -ATPase in the case of plants) and a Na+/H+ antiporter is one mechanism that confers salt tolerance to these organisms. The cloning and characterization of genes encoding these tonoplast transport proteins from crop plants may contribute to our understanding of how to enhance crop plant response to saline stress. We cloned wheat orthologs of the Arabidopsis genes AtNHX1 and AVP1 using the polymerase chain reaction and primers corresponding to conserved regions of the respective coding sequences, and a wheat cDNA library as template. The wheat NHX cDNA cloned by this approach was a variant of the previously reported TNHX1 gene. The vacuolar H+ -PPase pump we cloned (TVP1) is the first member of this gene family cloned from wheat; it is deduced translation product is homologous to proteins encoded by genes in barley, rice, and Arabidopsis. Function of TNHX1 as a cation/proton antiporter was demonstrated using the nhx1 yeast mutant. TNHX1 was capable of suppressing the hyg sensitivity of nhx1. Functional characterization of the wheat H+ -PPase TVP1 was demonstrated using the yeast ena1 (plasma membrane Na+ -efflux transporter) mutant. Expression of TVP1 in ena1 suppressed its Na+ hypersensitivity. Expression analysis of salt-stressed wheat plants showed substantial up-regulation of TNHX1 transcript levels as compared to control plants, while transcript accumulation for TVP1 was not greatly affected by exposure of plants to salt stress.
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PMID:Cloning and characterization of a wheat vacuolar cation/proton antiporter and pyrophosphatase proton pump. 1590 86

The effects of NaCl stress on the H+ -ATPase, H+ -PPase activity and lipid composition of plasma membrane (PM) and tonoplast(TP) vesicles isolated from roots and leaves of two soybean cultivars (Glycine max L.) differing in salt tolerance (Wenfeng7, salt-tolerant; Union, salt-sensitive) were investigated. When Wenfeng7 was treated with 0.3% (W/V) NaCl for 3 d, the H+ -ATPase activities in PM and TP from roots and leaves exhibited a reduction and an enhancement, respectively. The H+ -PPase activity in TP from roots also increased. Similar effects were not observed in roots of Union. In addition, the increases of phospholipid content and ratios of phospholipid to galactolipid in PM and TP from roots and leaves of Wenfeng7 may also change membrane permeability and hence affect salt tolerance.
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PMID:Effects of salinity on activities of H+ -ATPase, H+ -PPase and membrane lipid composition in plasma membrane and tonoplast vesicles isolated from soybean (Glycine max L.) seedlings. 1629 1

The vacuole is a large, multifunctional organelle related to the processes of cell expansion, solute accumulation, regulation of cytoplasmic ion concentrations, pH homeostasis and osmoregulation, which are directly or indirectly achieved by vacuolar H+-pumps: vacuolar H+-ATPase (V-ATPase; EC 3.6.1.3) and vacuolar H+-pyrophosphatase (V-PPase; EC 3.6.1.1). In this study, we produced antisense-transgenic tomatoes (Lycopersicon esculentum L.) of the V-ATPase A subunit, which is under the control of the fruit-specific 2A11 promoter. One beta-glucuronidase (GUS)-transgenic line (GUS control) and seven A subunit antisense-transgenic lines were obtained. The amount of V-ATPase A subunit mRNA in fruit decreased in all antisense-transgenic lines, but in leaves showed no difference compared with the GUS control line and the nontransformant, suggesting that suppression of the V-ATPase A subunit by a 2A11 promoter is limited to fruit. The antisense-transgenic plants had smaller fruits compared with the GUS control line and the nontransformant. Surprisingly, fruits from the antisense-transgenic plants, except the fruit that still had relatively high expression of A subunit mRNA, had few seeds. Sucrose concentration in fruits from the antisense-transgenic plants increased, but glucose and fructose concentrations did not change. These results show the importance of V-ATPase, not only in fruit growth, but also in seed formation and in sugar composition of tomato fruit.
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PMID:Fruit-specific V-ATPase suppression in antisense-transgenic tomato reduces fruit growth and seed formation. 1632 82

The effects of exogenous polyamines on the growth, polyamines contents, the activities of H(+)-ATPase and H(+)-PPase of plasma membrane and tonoplast in cucumber seedling roots under root-zone hypoxia stress were studied under hydroponic culture. The results showed that the growth of cucumber roots was significantly inhibited by hypoxia stress (Table 1). While the growth inhibition in cucumber roots by hypoxia stress could be alleviated by spraying exogenous polyamines. From these results (Table 1 and 2) we can conclude that Spd played an active physiological role in relieving hypoxia stress and Put exerted actively physiological role by enhancing Spd biosynthesis. The results also showed that the endogenous polyamine contents in cucumber roots were increased by hypoxia stress and spraying exogenous polyamines. Exogenous polyamines application obviously promoted the H(+)-ATPase activities of plasma membrane in cucumber roots (Fig.1), but did not significantly affect the H(+)-ATPase and H(+)-PPase activities of tonoplast in cucumber roots (Fig.2,3). The results suggested that exogenous polyamines could enhance hypoxia resistance of cucumber seedlings by increasing H(+)-ATPase activities of plasma membrane in cucumber roots.
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PMID:[Effects of exogenous polyamines on the growth and activities of H+-ATPase and H+-PPase in cucumber seedling roots under hypoxia stress]. 1636 92

The chenopodiaceae Suaeda salsa L. is a leaf succulent euhalophyte. Shoots of the S. salsa are larger and more succulent when grown in highly saline environments. This increased growth and water uptake has been correlated with a large and specific cellular accumulation of sodium. S. salsa does not have salt glands or salt bladders on its leaves. Thus, this plant must compartmentalize the toxic Na(+) in the vacuoles. The ability to compartmentalize sodium may result from a stimulation of the proton pumps that provide the driving force for increased sodium transport into the vacuole. In this work, we isolated the cDNA of the vacuolar membrane proton-translocating inorganic pyrophosphatase (H(+) -PPase) from S. salsa. The SsVP cDNA contains an uninterrupted open reading frame of 2292 bp, coding for a polypeptide of 764 amino acids. Northern blotting analysis showed that SsVP was induced in salinity treated leaves. The activities of both the V-ATPase and the V-PPase in Arabidopsis overexpressing SsVP-2 is higher markedly than in wild-type plant under 200 mM NaCl and drought stresses. The Overexpression of SsVP can increase salt and drought tolerance of transgenic Arabidopsis.
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PMID:Molecular cloning and characterization of a vacuolar H+ -pyrophosphatase gene, SsVP, from the halophyte Suaeda salsa and its overexpression increases salt and drought tolerance of Arabidopsis. 1646 98

Si 2.0 mmol/L in irrigation solution alleviated significantly the inhibition of NaCl stress of 100 or 200 mmol/L to aloe growth. Exogenously applied Si decreased significantly Na(+) and Cl(-) contents, increased K(+) content and K(+)/Na(+) ratio and selectivity ratio of absorption (AS(K, Na)) and of translocation (TS(K, Na)) to K(+) and Na(+) in aloe plant under both NaCl 100 and 200 mmol/L stresses for 30 d. In this way, the ion homeostasis in aloe plant under NaCl stress was maintained, as was proved by X-ray microanalysis of root tip and leaf across sections. One of the mechanisms to achieve this may be the significant enhancement of H(+)-ATPase activities by the addition of silicate in plasma membrane and tonoplast, H(+)-pyrophosphatase (H(+)-PPase) activity in tonoplast isolated from aloe root tips under NaCl stress.
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PMID:Silicate improves growth and ion absorption and distribution in aloe vera under salt stress. 1647 34

Nitric oxide (NO), an endogenous signaling molecule in animals and plants, mediates responses to abiotic and biotic stresses. Our previous work demonstrated that 100 microM sodium nitroprusside (SNP, an NO donor) treatment of maize seedlings increased K(+) accumulation in roots, leaves and sheathes, while decreasing Na(+) accumulation (Zhang et al. in J Plant Physiol Mol Biol 30:455-459, 2004b). Here we investigate how NO regulates Na(+), K(+) ion homeostasis in maize. Pre-treatment with 100 muM SNP for 2 days improved later growth of maize plants under 100 mM NaCl stress, as indicated by increased dry matter accumulation, increased chlorophyll content, and decreased membrane leakage from leaf cells. An NO scavenger, methylene blue (MB-1), blocked the effect of SNP. These results indicated that SNP-derived NO enhanced maize tolerance to salt stress. Further analysis showed that NaCl induced a transient increase in the NO level in maize leaves. Both NO and NaCl treatment stimulated vacuolar H(+)-ATPase and H(+)-PPase activities, resulting in increased H(+)-translocation and Na(+)/H(+) exchange. NaCl-induced H(+)-ATPase and H(+)-PPase activities were diminished by MB-1. 1-Butanol, an inhibitor of phosphatidic acid (PA) production by phospholipase D (PLD), reduced NaCl- and NO-induced H(+)-ATPase activation. In contrast, applied PA stimulated H(+)-ATPase activity. These results suggest that NO acts as a signal molecule in the NaCl response by increasing the activities of vacuolar H(+)-ATPase and H(+)-PPase, which provide the driving force for Na(+)/H(+) exchange. PLD and PA play an important role in this process.
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PMID:Nitric oxide enhances salt tolerance in maize seedlings through increasing activities of proton-pump and Na+/H+ antiport in the tonoplast. 1650 90

Sodium nitroprusside (SNP) could ameliorate the inhibition effect of Al on root growth of rye (Secale cereale L. cv. King) and wheat (Triticum aestivum L. cv. Jinmai47). Respiratory rate, P/O, OPR (oxygenated phosphate rate), R(3) (oxygen consumption rate with ADP and substrate present), R(4) (oxygen consumption rate with substrate) and RCR (respiratory control ratio, R(3)/R(4)) of root tips from rye and wheat decreased, as well as the activities of H(+)-ATPase, H(+)-PPase, Na(+)-K(+)-ATPase, Ca(2+)-ATPase and Mg(2+)-ATPase, but they increased with SNP treatment. It showed that mitochondrial respiratory functions of root tips from rye and wheat were damaged, phosphorylation was un-coupled by Al, but that of rye was less than that of wheat. Rye has high Al-resistance ability than wheat. SNP is one of donor of NO, it is suggested that NO can ameliorate remarkably respiratory dysfunction resulted from Al stress, so that NO can ameliorate the inhibition effect of Al on plant growth.
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PMID:[Effects of sodium nitroprusside on mitochondrial function of rye and wheat root tip under aluminum stress]. 1662 25

The H(+)-translocating inorganic pyrophosphatase (H(+)-PPase) associated with vesicles of the vacuolar membrane (tonoplast) isolated from beet (Beta vulgaris L.) is subject to direct inhibition by Ca(2+) and a number of other divalent cations (Co(2+), Mn(2+), Zn(2+)). By contrast, the H(+)-translocating ATPase (H(+)-ATPase) located on the same membrane is insensitive to Ca(2+). Here we examine the mechanism and feasibility of regulation of the vacuolar H(+)-PPase by cytosolic free Ca(2+) under the conditions thought to prevail in vivo with respect to Mg(2+), inorganic pyrophosphate (PPi), and pH. The minimal reaction scheme that satisfactorily describes the effects of elevated Ca(2+) or CaPPi on the enzyme is one that invokes equilibrium binding of substrate (Mg(2)PPi) at one site, inhibitory binding of Mg(2)PPi to a lower-affinity second site, binding of activator (Mg(2+)) at a third site, and direct binding of Ca(2+) or CaPPi to a fourth site. Changes in enzyme activity in response to selective manipulation of either Ca(2+) or CaPPi are explicable only if Ca(2+), rather than CaPPi, is the inhibitory ligand. This conclusion is supported by the finding that CaPPi fails to mimic substrate in protection of the enzyme from inhibition by N-ethylmaleimide. Furthermore, the reaction scheme quantitatively and independently predicts the observed noncompetitive effects of free Ca(2+) on the substrate concentration dependence of H(+)-PPase activity. The results are discussed in relation to the previous proposal that CaPPi is the principal inhibitory ligand of the vacuolar H(+)-PPase (M. Maeshima [1991] Eur J Biochem 196: 11-17) and the possibility that in vivo modulation of cytosolic free Ca(2+) might constitute a specific mechanism for selective regulation of this enzyme, and consequently for stabilization of PPi levels in the cytoplasm of plant cells.
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PMID:Regulation of vacuolar h-pyrophosphatase by free calcium : a reaction kinetic analysis. 1665 87


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