Salt modulation of vacuolar H+-ATPase and H+-Pyrophosphatase activities in Vigna unguiculata
| Autor: | Alana Cecília Menezes Sobreira, Maria Erivalda Farias de Aragão, Maria de Lourdes Oliveira Otoch, Dirce Fernandes de Melo, Maria da Guia Silva Lima, Elena G. Orellano |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
chemistry.chemical_classification
Pyrophosphatase biology medicine.diagnostic_test Physiology Sodium ATPase chemistry.chemical_element Plant Science Vacuole biology.organism_classification Vigna chemistry.chemical_compound Enzyme chemistry Western blot Biochemistry Proton transport biology.protein medicine Agronomy and Crop Science |
| Zdroj: | Journal of Plant Physiology. 158:545-551 |
| ISSN: | 0176-1617 |
| DOI: | 10.1078/0176-1617-00310 |
| Popis: | Summary Salt modulation of the tonoplast H+-pumping V-ATPase and H+-PPase was evaluated in hypocotyls ofVigna unguiculata seedlings after 3 and 7 days of treatment. In 3-day-old seedlings, treatment with 100 mmol/L NaCl decreased the proton transport and hydrolytic activities of both the V-ATPase and the H+-PPase. After 7 days, the proton transport and hydrolysis activities of the V-ATPase were higher, while the H+-PPase activities were lower in seedlings. Western blot analysis of A- and B-subunits of V-ATPase revealed that the protein content of the two subunits varied in parallel with their activities, i.e. to a higher activity corresponded a higher protein content of the subunits and vice versa. Contrarily, Western blot analysis of H+-PPase levels failed to show any correlation with PPase activity, suggesting a partial enzyme inactivation. The results indicate that salt stress induces V-ATPase expression inV. unguiculata with concomitant enhancement of its activity as a homeostatic mechanism to cope with salt stress. Under the same conditions PPase is inhibited. |
| Databáze: | OpenAIRE |
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