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)

Fusicoccin (FC) is a well known toxin acting as a 14-3-3 protein-mediated activator of the plasma membrane H(+)-ATPase and the biochemical and physiological changes induced in the cell by this toxin have, up to now, been ascribed to the increased rate of proton extrusion by this pump leading to external acidification and cell hyperpolarization. In a recent work (Malerba M et al. 2003, Physiologia Plantarum, 119: 480-488) it was shown that, besides the previously well studied changes, FC induces a large stimulation of H(2)O(2) production, an activation of alternative respiration and a leakage of cytochrome c from mitochondria. In this article further studies on the relation between the H(2)O(2) overproduction and medium acidification are reported. The increase in the rate of H(2)O(2) accumulation is particularly evident when high concentrations of the toxin ensure a rapid acidification of the medium, but it is not obtained when the time-course of acidification is reproduced by external acid additions. The FC-dependent H(2)O(2) overproduction is strongly inhibited by inhibitors of the H(+)-ATPase activity, such as vanadate and erythrosin B, and it does not occur when the activation of the H(+)-ATPase is prevented by phenylarsine oxide (PAO), an inhibitor of the activating interaction between the enzyme and its regulative 14-3-3 protein. Interestingly, all these inhibitors only partially prevent the leakage of cytochrome c from the mitochondria. A kinetic analysis of FC-dependent changes of 14-3-3s shows that the initial increase in the plasma membrane level of these proteins, presumably due to translocation of free cytosolic forms, is followed by a remarkable increase in the level of the 14-3-3 proteins located in the cytosol. This latter change is not prevented by inhibitors of the activity or activation of the H(+)-ATPase. These results suggest that, besides the H(+)-ATPase activation, FC can induce other cell changes possibly mediated by changes of the regulative 14-3-3 proteins.
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PMID:Fusicoccin affects cytochrome c leakage and cytosolic 14-3-3 accumulation independent of H-ATPase activation. 1503 35

Reactive oxygen species (ROS) in the apoplast of cells in the growing zone of grass leaves are required for elongation growth. This work evaluates whether salinity-induced reductions in leaf elongation are related to altered ROS production. Studies were performed in actively growing segments (SEZ) obtained from leaf three of 14-d-old maize (Zea mays L.) seedlings gradually salinized to 150 mM NaCl. Salinity reduced elongation rates and the length of the leaf growth zone. When SEZ obtained from the elongation zone of salinized plants (SEZs) were incubated in 100 mM NaCl, the concentration where growth inhibition was approximately 50%, O2*- production, measured as NBT formazan staining, was lower in these than in similar segments obtained from control plants. The NaCl effect was salt-specific, and not osmotic, as incubation in 200 mM sorbitol did not reduce formazan staining intensity. SEZs elongation rates were higher in 200 mM sorbitol than in 100 mM NaCl, but the difference could be cancelled by scavenging or inhibiting O2*- production with 10 mM MgCl2 or 200 microM diphenylene iodonium, respectively. The actual ROS believed to stimulate growth is *OH, a product of O2*- metabolism in the apoplast. SEZ(s) elongation in 100 mM NaCl was stimulated by a *OH-generating medium. Fusicoccin, an ATPase stimulant, and acetate buffer pH 4, could also enhance elongation in these segments, although both failed to increase ROS activity. These results show that decreased ROS production contributes to the salinity-associated reduction in grass leaf elongation, acting through a mechanism not associated with pH changes.
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PMID:Decreased reactive oxygen species concentration in the elongation zone contributes to the reduction in maize leaf growth under salinity. 1515 79

Plant plasma membrane H+-ATPases (PMAs) can be activated by phosphorylation of their penultimate residue (a Thr) and the subsequent binding of regulatory 14-3-3 proteins. Although 14-3-3 proteins usually exist as dimers and can bind two targets, the in vivo effects of their binding on the quaternary structure of H+-ATPases have never been examined. To address this question, we used a Nicotiana tabacum cell line expressing the Nicotiana plumbaginifolia PMA2 isoform with a 6-His tag. The purified PMA2 was mainly nonphosphorylated and 14-3-3-free, and it was shown by blue native gel electrophoresis and chemical cross-linking to exist as a dimer. Fusicoccin treatment of the cells resulted in a dramatic increase in Thr phosphorylation, 14-3-3 binding, and in vivo and in vitro ATPase activity, as well as in the conversion of the dimer into a larger, possibly hexameric, complex. PMA2 phosphorylation and 14-3-3 binding were observed also when cells in stationary growth phase were metabolically activated by transfer to fresh medium. When expressed in yeast, PMA2 was also phosphorylated and formed a complex with 14-3-3 proteins without requiring fusicoccin; no complex was observed when phosphorylation was prevented by mutagenesis. Single-particle analysis by cryoelectron microscopy showed that the PMA2-14-3-3 complex is a wheel-like structure with a 6-fold symmetry, suggesting that the activated complex consists of six H+-ATPase molecules and six 14-3-3 molecules.
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PMID:Activation of the plant plasma membrane H+-ATPase by phosphorylation and binding of 14-3-3 proteins converts a dimer into a hexamer. 1608 36

We investigated the responses of stomata to light in the fern Adiantum capillus-veneris, a typical species of Leptosporangiopsida. Stomata in the intact leaves of the sporophytes opened in response to red light, but they did not open when blue light was superimposed on the red light. The results were confirmed in the isolated Adiantum epidermis. The red light-induced stomatal response was not affected by the mutation of phy3, a chimeric protein of phytochrome and phototropin in this fern. The lack of a blue light-specific stomatal response was observed in three other fern species of Leptosporangiopsida, i.e. Pteris cretica, Asplenium scolopendrium and Nephrolepis auriculata. Fusicoccin, an activator of the plasma membrane H(+)-ATPase, induced both stomatal opening and H(+) release in the Adiantum epidermis. Adiantum phototropin genes AcPHOT1 and AcPHOT2 were expressed in the fern guard cells. The transformation of an Arabidopsis phot1 phot2 double mutant, which lost blue light-specific stomatal opening, with AcPHOT1 restored the stomatal response to blue light. Taken together, these results suggest that ferns of Leptosporangiopsida lack a blue light-specific stomatal response, although the functional phototropin and plasma membrane H(+)-ATPase are present in this species.
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PMID:The fern Adiantum capillus-veneris lacks stomatal responses to blue light. 1662 42

p-Chloromercuribenzenesulfonic acid markedly inhibited sucrose accumulation into sugar beet source leaves without inhibiting hexose accumulation. The site of inhibition is proposed to be the plasmalemma ATPase, since the ATPase-mediated H(+) efflux was completely inhibited by p-chloromercuribenzenesulfonic acid under conditions where intracellular metabolism, as measured by photosynthesis and hexose accumulation, was unaffected. Fusicoccin, a potent activator of active H(+)/K(+) exchange, stimulated both active sucrose accumulation and proton efflux in the sugar beet leaf tissue. These data provide strong evidence for the phloem loading of sucrose being coupled to a proton transport mechanism driven by a vectorial plasmalemma ATPase.
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PMID:Phloem loading of sucrose: involvement of membrane ATPase and proton transport. 1666 Aug 4

The block in the electrogenic H(+) efflux produced by protein synthesis inhibitors in corn root tissue can be released or by-passed by addition of fusicoccin or nigericin. The inhibition also lowers cell potential, and the release repolarizes. Associated with the inhibition of H(+) efflux is inhibition of K(+) influx and the growth of the root tip; fusicoccin partially relieves these inhibitions, but nigericin does not. The inhibition of H(+) efflux which arises from blocking the proton channel of the ATPase by oligomycin or N,N'-dicyclohexylcarbodiimide can also be partially relieved by fusicoccin, but not by nigericin; the inhibition produced by diethylstilbestrol is not relieved by fusicoccin.The results are discussed in terms of the presumed mode of action of fusicoccin on the plasmalemma ATPase. Inhibition of protein synthesis appears to inactivate the proton channel of the ATPase, possibly as the indirect result of disrupted metabolism. Fusicoccin reactivates or bypasses the blocked channel.
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PMID:Action of protein synthesis inhibitors in blocking electrogenic h efflux from corn roots. 1666 63

Recent experiments show that exogenous NADH increases the O(2) consumption and uptake of inorganic ions into isolated corn (Zea mays L. Pioneer Hybrid 3320) root protoplasts (Lin 1982, Proc Natl Acad Sci USA 79: 3773-3776). A mild treatment of protoplasts with trypsin released most of the NADH oxidation system from the plasmalemma (Lin 1982 Plant Physiol 70: 326-328). Further studies on this system showed that exogenous NADH (1.5 millimolar) tripled the proton efflux from the protoplasts thus generating a greater electrochemical proton gradient across the plasmalemma. Trypsin also released ubiquinone (11.95 nanomoles per milligrams protein) but not flavin or cytochrome from the system. Kinetic analyses showed that 1.5 millimolar NADH quadrupled V(max) of the mechanism I (saturable) component of K(+) uptake, while K(m) was not affected. Diethylstibestrol and vanadate inhibited basal (ATPase-mediated) K(+) influx and H(+) efflux, while NADH-stimulated K(+) uptake was not or only slightly inhibited. p-Chloromercuribenzene-sulfonic acid, N,N'-dicyclohexylcarbodiimide, ethidium bromide, and oligomycin inhibited both ATPase- and NADH-mediated H(+) and K(+) fluxes. A combination of 10 millimolar fusicoccin and 1.5 millimolar NADH gave an 11-fold increase of K(+) influx and a more than 3-fold increase of H(+) efflux. It is concluded that a plasmalemma ATPase is not involved in the NADH-mediated ion transport mechanism. NADH oxidase is a -SH containing enzyme (protein) and the proton channel is an important element in this transport system. Fusicoccin synergistically stimulates the effect of NADH on K(+) uptake.
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PMID:Further Characterization on the Transport Property of Plasmalemma NADH Oxidation System in Isolated Corn Root Protoplasts. 1666

Washing corn (Zea mays L.) root tissue in water causes loss of about one-third of the exchangeable Ca(2+) over the first 10 to 15 minutes. Upon transfer to K(+)-containing solutions, the tissue shows a short period of rapid K(+) influx which subsequently declines. Addition of 0.1 millimolar Ca(2+) decreases the initial rapid K(+) influx, but increases the sustained rate of K(+) and Cl(-) uptake. It was confirmed (Elzam and Hodges 1967 Plant Physiol 42: 1483-1488) that 0.1 millimolar Ca(2+) is more effective than higher concentrations for the initial inhibition, and that Mg(2+) will substitute.The inhibition arises from a mild shock affect of restoring Ca(2+). With 0.1 millimolar Ca(2+) net H(+) efflux is blocked for 10 to 15 minutes and the cells are depolarized by about 30 millivolts. However, 1 millimolar Ca(2+) rapidly produces increased K(+) influx and blocks net H(+) efflux for only a few minutes; blockage is preceded by a brief net H(+) influx which may restore and increase ion transport by reactivating the plasmalemma H(+)-ATPase.Stimulation of electrogenic H(+)-pumping with fusicoccin eliminates the shock responses and minimizes Ca(2+) effects on K(+) influx. Fusicoccin also strongly decreases Ca(2+) influx, but has no effect on Ca(2+) efflux. Ice temperatures and high pH decreased Ca(2+) efflux, but uncoupler and chlorpromazine did not.It is suggested that the inhibitory and promotive actions of Ca(2+) are manifested through decreases or increases in the protonmotive force.
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PMID:Reactions of corn root tissue to calcium. 1666 54

Proton extrusion by roots of intact sunflower plants (Helianthus annuus L.) was studied in nutrient solutions or in agar media with a pH indicator. Proton extrusion was enhanced by either iron deficiency, addition of fusicoccin, or single salt solutions of ammonium or potassium salts. The three types of proton extrusion differ in both localization along the roots and capacity. From their sensitivity to ATPase inhibitors it seems justified to characterize them as proton pumps driven by plasma membrane APTases.Enhanced proton extrusion induced by preferential cation uptake from (NH(4))(2)SO(4) or K(2)SO(4) was uniformly distributed over the whole root system. In contrast, the enhancement effect of fusicoccin was confined to the basal root zones and that of iron deficiency to the apical root zones. Also the rates of proton extrusion per unit of root fresh weight differed remarkably and increased in the order: Fusicoccin << K(2)SO(4) < (NH(4))(2)SO(4) < iron deficiency.Under iron deficiency the average values of proton extrusion for the whole root system are 5.6 micromoles H(+) per gram fresh weight per hour; however, for the apical root zones values of about 28 micromoles H(+) can be calculated. This high capacity is most probably related to the iron deficiency-induced formation of rhizodermal transfer cells in the apical root zones. It can be assumed that the various types of root-induced acidification of the rhizosphere are of considerable ecological importance for the plant-soil relationships in general and for mobilization of mineral nutrients from sparingly soluble sources in particular.
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PMID:Localization and capacity of proton pumps in roots of intact sunflower plants. 1666 91

The effect of fusicoccin on Mg:ATP-dependent H(+)-pumping in microsomal vesicles from 24-hour-old radish (Raphanus sativus L.) seedlings was investigated by measuring the initial rate of decrease in the absorbance of the DeltapH probe acridine orange. Fusicoccin stimulated Mg:ATP-dependent H(+)-pumping when the pH of the assay medium was in the range 7.0 to 7.6 while no effect of fusicoccin was detected between pH 6.6 and pH 6.0. Both basal and fusicoccin-stimulated H(+)-pumping were completely inhibited by vanadate and almost unaffected by nitrate. Fusicoccin did not change membrane permeability to protons and fusicoccin-induced stimulation of Mg:ATP-dependent H(+)-pumping was not affected by changes in the buffer capacity of the incubation medium. Deacetylfusicoccin stimulated H(+)-pumping as much as fusicoccin, while the physiologically inactive derivative 8-oxo-9-epideacetylfusicoccin did not. Stimulation of H(+)-pumping was saturated by 100 nanomolar fusicoccin. These data indicate that fusicoccin activates the plasma membrane H(+)-ATPase by acting at the membrane level independently of the involvement of other cell components. The percent stimulation by fusicoccin was the same at all ATP concentrations tested (0.5-5.0 millimolar), thus suggesting that with fusicoccin there is an increase in V(max) of the plasma membrane H(+)-ATPase rather than a decrease in its apparent K(m) for Mg:ATP.
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PMID:H-pumping driven by the plasma membrane ATPase in membrane vesicles from radish: stimulation by fusicoccin. 1666 78


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