Complementation of the Saccharomyces cerevisiaePlasma Membrane H+-ATPase by a Plant H+-ATPase Generates a Highly Abundant Fusicoccin Binding Site
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Fusicoccin Activates the Plasma Membrane H+-ATPase by a Mechanism Involving the C-Terminal Inhibitory Domain.
Plasma membrane vesicles isolated from spinach leaves incubated with the fungal toxin fusicoccin showed a twofold increase in ATP hydrolytic activity and a threefold increase in H+ pumping compared to controls. This increase in H+-ATPase activity was largely completed within 4 min of incubation and was not due to de novo synthesis of H+-ATPase as demonstrated by immunoblotting. Incubation with ...
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The present study was conducted to find the effect of three heavy metals, Ag, Hg and Pb on the expression level of a gene encoding plasma membrane H+-ATPase in Aeluropus littoralis. The experiment was laid out in a completely random design with three replications. The expression of the main gene was normalized to the expression of the housekeeping gene actin. Two 259 and 187 bp fragments were a...
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Michel Ronjat, Jean Jacques Lacapere$, Jean-Pierre Dufourp, and Yves Dupont From the Luboratoire de Bwphysique Mol=Gculaire et Cellulaire, Centre d’Etudes Nuckaires de Grenoble, 3804l-Grenoble, France, the $Service de Biophysique, Departement de Biologic, Centre d’Etudes Nuckaires de Saclay, 91190-Gif-sur-Yuette, France, and the ILabOratoire des Sciences et Technologies Brassicoles, Uniuersite ...
متن کاملThe fluorescein isothiocyanate-binding site of the plasma-membrane H+-ATPase of Neurospora crassa.
The mammalian (Na+,K+), Ca2+-, and (H+,K+)-ATPases contain a well-characterized lysine residue that reacts with fluorescein 5'-isothiocyanate (FITC); enzymatic activity is protected by ATP, suggesting that the residue is located in or near the nucleotide-binding domain. In this study, the plasma-membrane H+-ATPase of Neurospora crassa is also shown to be sensitive to FITC. The reaction occurs w...
متن کاملProteolytic activation of the plant plasma membrane H(+)-ATPase by removal of a terminal segment.
Incubation of oat root plasma membrane vesicles in the presence of ATP with trypsin or chymotrypsin increased the rate of ATP hydrolysis and ATP-dependent proton pumping by the plasma membrane H(+)-ATPase. Proton pumping was stimulated more than 200%, whereas ATP hydrolytic activity was stimulated about 30%. The Km (ATP) for both proton pumping and ATP hydrolysis was lowered from about 0.3 mM t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1998
ISSN: 0021-9258
DOI: 10.1074/jbc.273.45.30018