ATPases Associated with Membranes of Plant Cells

Hodges, Thomas K.

doi:10.1007/978-3-642-66227-0_10

Cited by 83 publications

(144 citation statements)

References 42 publications

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“…Although anion-stimulated ATPase activity has been reported to be present in some plasma membrane preparations (e.g. 8), the plasma membrane ATPase of corn roots does appear to be potassium-stimulated (9). In oat roots, the potassium-stimulated ATPase was distributed mainly in the pellet of the dextran step gradient, while the interface vesicles were enriched in a chloridestimulated activity (26).…”

Section: Resultsmentioning

confidence: 92%

Localization of the Proton Pump of Corn Coleoptile Microsomal Membranes by Density Gradient Centrifugation

Mandala¹,

Mettler²,

Taiz³

1982

Plant Physiol.

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Previous studies characterizing an ATP-dependent proton pump in microsomal membrane vesicles of corn coleoptiles led to the conclusion that the proton pump was neither mitochondrial nor plasma membrane in origin Plant Physiol 70: 1738-1742. To facilitate positive identification of the vesicles, corn coleoptile microsomal membranes were fractionated on linear sucrose and dextran gradients, with ATP-dependent j'4Clmethylamine uptake as a probe for proton pumping. On sucrose gradients, proton pumping activity exhibited a density of 1.11 grams/cubic centimeter and was coincident with the endoplasmic reticulum (ER). In the presence of high magnesium, the ER shifted to a heavier density, while proton pumping activity showed no density shift. On linear dextran gradients, proton pumping activity peaked at a lighter density than the ER. The proton pump appears to be electrogenic since both I14CISCN-uptake and 3Cl-uptake activities coincided with I'4C1 methylamine uptake on dextran gradients. On the basis of density and transport properties, we conclude that the proton pumping vesicles are probably derived from the tonoplast. Nigericin-stimulated ATPase activity showed a broad distribution which did not coincide with any one membrane marker.

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Section: Resultsmentioning

confidence: 92%

Localization of the Proton Pump of Corn Coleoptile Microsomal Membranes by Density Gradient Centrifugation

Mandala¹,

Mettler²,

Taiz³

1982

Plant Physiol.

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“…Substantial evidence, although indirect, suggests that an ATPase in higher plants is also involved in H+ extrusion and K+ uptake (15). (a) There is a good correlation between K+ uptake in vivo and K+-stimulated ATPase activity in vitro in various plant materials (7). K+ uptake and ATPase activity show similar kinetics as a function of K+ concentration (7).…”

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confidence: 99%

Relationship between ATP Level and Activity of Fusicoccin-stimulated H⁺/K⁺-Exchange System in Plant Tissues

Rasi‐Caldogno¹,

Cerana²,

Pugliarello³

1980

Plant Physiol.

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The treatment with fusicoccin causes a slight but significant decrease (about 15%) The electrogenic proton extrusion stimulated by FC1 is an energy-dependent process which is inhibited by respiratory and metabolic poisons (12,16). Recent data indicate that, in Neurospora (18,19) and in bacteria (6), ATP is the energy source for electrogenic transport systems presumably analogous to the one activated by FC in higher plants. Substantial MATERIALS AND METHODS Maize (Zea mays L. cv. Dekalb XL 640) seeds and peak (Pisum sativum cv. Alaska) seedlings were grown for 4 and 6 days, respectively, at 26 C on poplar sawdust in the dark.Maize-coleoptile segments, 3 mm long, were cut from the region between 5 and 15 mm from the tip; the segments were longitudinally divided in half. Pea-stem segments, 2 mm long, were cdt in the subapical region of the distal internode. The segments were washed for 2 h in 0.5 mm CaCl2 and 0.25 nuM MgCl2 (the solution was changed after 30 min) and then transferred to the various media as described in the individual experiments; 0.5 mM CaCl2 and 0.25 mM MgCl2 were present in every treatment. The experiments were run in the dark in a thermoregulated water-bath with shaking (70 shakes/min) at 28 C in the case of maize coleoptiles and at 25 C in the case of pea-stem segments.An atmosphere of 3% 02 or anaerobiosis was obtained by continuous bubbling in the incubation medium of 3% 02-97% N2 or of 02-free N2.Three different methods of ATP extraction from the tissue were tested: incubation in boiling triethanolamine HCl/NaOH buffer (pH 7.6) for 1 min (5), treatment with liquid N2 and 5% trichloroacetic acid containing 0.05% 8-hydroxyquinoline, and treatment with 0.8 N HC104 at 0 C. The tissue was always homogenized in a mortar in the presence of sea sand. The highest values of ATP levels were obtained by extraction with 0.8 N HC104 at 0 C, therefore, this extraction was performed in all the experiments.The 3% 02 atmosphere and anaerobiosis were maintained during fixation ofthe tissue with HC104. The homogenate was centrifuged for 5 min and the pellet was washed with 0.8 N HC104. The two supernatants were combined, neutralized with KOH in the presence of 120 mM triethanolamine HCl/NaOH buffer (pH 7.6), and centrifuged again. The enzymic assay of ATP was performed on the supernatant according to Lamprecht and Trautshold (10). K+ uptake was assayed by using rubidium-86 as a tracer. Incubation was performed in 1 mm KCI labeled with 0.5 ,uCi mRbCl; at the end of the incubation, the tissue was briefly rinsed with 10 ml cold unlabeled solution and then washed at 0 C for 10 min in 5 ml ice-cold unlabeled solution; finally, the sections were rapidly rinsed with ice-cold H20. Distilled H20 (4 ml) and 10 ml Instagel (Packard) were added to the tissue and the radioactivity of the samples was measured in a Packard Tri-Carb scintillation

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“…If these phosphatases are truly ATPases, as are those of Albers & Koval (1972), then they are of considerable interest to those working with transport phenomena (Hodges, 1976), and to those who find evidence that these enzymes may be the primary site of attack by the pathogen's metabolites (Phillips et al, 1978;Steele et al, 1978;Mondal, 1978;Selman & Durbin, 1978). This is because ATPases are considered to be part of a critical support and supply system of the plant cells (Hodges, 1976).…”

Section: Resultsmentioning

confidence: 99%

“…Cell-wall phosphatases have been reported (Wainwright & Woolhouse, 1978), and their activity may be a reflection of the presence of ATPase associated with the cell wall (Hooper et al, 1978;Hall & Butt, 1969;Hall, 1971;Al-Azzawi & Hall, 1977). If these phosphatases are truly ATPases, as are those of Albers & Koval (1972), then they are of considerable interest to those working with transport phenomena (Hodges, 1976), and to those who find evidence that these enzymes may be the primary site of attack by the pathogen's metabolites (Phillips et al, 1978;Steele et al, 1978;Mondal, 1978;Selman & Durbin, 1978). This is because ATPases are considered to be part of a critical support and supply system of the plant cells (Hodges, 1976).…”

Section: Resultsmentioning

confidence: 99%

“…In view of this, the inhibition of phosphatase is an effect independent from the increase in susceptibility to Verticillium that follows Kelthane application. However, since the cell-wall phosphatases are believed to be part of the plant's transport complex (Hodges, 1976), and the wilt symptoms of the disease are indicative of disruption of these transport activities (Dimond, 1970;Basham & Bateman, 1975), it seems reasonable to consider a common linkage between the two Kelthane effects: the loss of M-8 variety's weak tolerance to Verticillium wilt and the inhibition of the cell-wall phosphatase. Yet it is premature to consider the matter further until more information on the system is obtained.…”

Section: Resultsmentioning

confidence: 99%

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The cell-wall phosphatase of cotton (Gossypium) is inhibited by kelthane

Daley¹,

Carroll²,

Mussell³

1979

Biochemical Journal

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Kelthane [4,4′-dichloro-alpha-(trichloromethyl)benzhydrol] was previously shown to decrease the limited tolerance of susceptible varieties of cotton (Gossypium) to Verticillium wilt. Kelthane was shown in the present study to inhibit the cell-wall p-nitrophenyl phosphatase of cotton. In view of information already establishing the cell wall as a primary site of action of Verticillium wilt, the data are interpreted as suggesting an as yet undefined interaction between Kelthane, cell-wall phosphatase and verticillium-resistance mechanisms of the cell wall.

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ATPases Associated with Membranes of Plant Cells

Cited by 83 publications

References 42 publications

Localization of the Proton Pump of Corn Coleoptile Microsomal Membranes by Density Gradient Centrifugation

Localization of the Proton Pump of Corn Coleoptile Microsomal Membranes by Density Gradient Centrifugation

Relationship between ATP Level and Activity of Fusicoccin-stimulated H⁺/K⁺-Exchange System in Plant Tissues

The cell-wall phosphatase of cotton (Gossypium) is inhibited by kelthane

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ATPases Associated with Membranes of Plant Cells

Cited by 83 publications

References 42 publications

Localization of the Proton Pump of Corn Coleoptile Microsomal Membranes by Density Gradient Centrifugation

Localization of the Proton Pump of Corn Coleoptile Microsomal Membranes by Density Gradient Centrifugation

Relationship between ATP Level and Activity of Fusicoccin-stimulated H+/K+-Exchange System in Plant Tissues

The cell-wall phosphatase of cotton (Gossypium) is inhibited by kelthane

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Relationship between ATP Level and Activity of Fusicoccin-stimulated H⁺/K⁺-Exchange System in Plant Tissues