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Fungal Genet Biol. 1996 Mar;20(1):30-5.

Plasma Membrane H+-ATPase Activity in Spores, Germ Tubes, and Haustoria of the Rust Fungus Uromyces viciae-fabae

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Lehrstuhl fur Phytopathologie, Universitat Konstanz, Konstanz, 78 434, Germany


Using plasma membrane-enriched vesicles, the properties of the H+-ATPase (EC from the rust fungus Uromyces viciae-fabae were studied. The enzyme is strictly Mg2+-dependent and is inhibited by vanadate. The pH-optimum is at 6.7. By Western blot analysis using a monoclonal antibody against corn plasma membrane H+-ATPase a polypeptide of approximately 104 kDa could be detected. The vanadate-sensitive H+-ATPase activity of microsomal vesicles obtained from different stages of rust development was determined. Uredospores had only a very low enzyme activity (1.9 μmol Pi x mg-1 protein x h-1). In germ tubes the ATPase activity was about twofold higher (4.0 μmol Pi x mg-1 protein x h-1). An eightfold higher ATPase activity (16.1 μmol Pi x mg-1 protein x h-1) was found in microsomal vesicles from haustoria which had been isolated from rust-infected Vicia faba leaves. These results suggest, that the electrochemical gradient generated by the H+-ATPase of haustoria plays an important role for their function, possibly by promoting nutrient uptake from host cells.


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