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Dynamics of activity and structure of the tonoplast vacuolar-type H+-ATPase in plants with differing CAM expression and in a C3 plant under salt stress

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Summary

Differences in the activity and structure of the vacuolar H+-ATPase (V-ATPase, EC 3.6.1.3) were investigated in the C3/CAM intermediate plantKalanchoë blossfeldiana Poellnitz cv. Tom Thumb, with lower or higher expression of CAM, andHordeum vulgare cv. Carina, grown with or without 150 mM NaCl. InK. blossfeldiana ATP-hydrolysis and H+-transport activity were higher with higher expression of CAM than in plants with very weak CAM. This was mainly due to a larger amount of V-ATPase. Statistical analysis of the diameter of intramembrane particles (IMPs) on freeze-fractures of tonoplast vesicles showed that IMPs were larger in tonoplast vesicle preparations ofK. blossfeldiana with strong CAM expression (9.1 nm) than in preparations ofK. blossfeldiana with low CAM expression (7.3 nm). As there is evidence that the majority of IMPs on freeze-fractures of tonoplast vesicles corresponds to the V0 domain of V-ATPase, the higher activity of V-ATPase inK. blossfeldiana with stronger CAM could be a result of additional structural changes in its membrane-integral domain. The higher activity of V-ATPase inK. blossfeldiana with stronger CAM is discussed in relation to the requirement for a higher proton pumping capacity for nocturnal malate accumulation in the vacuole. The ATP-dependent H+-pumping activity inH. vulgare was higher under salt stress than in control plants, while the rates of ATP-hydrolysis and the size of IMPs were not affected by the salt treatment. The data presented here indicate that different mechanisms might increase the transport capacity of V-ATPase to meet the higher requirements of secondary active transport related to CAM expression and adaptation to salt stress.

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Abbreviations

ATP:

adenosine triphosphate

CAM:

crassulacean acid metabolism

IMP:

intramembrane particles

V-ATPase:

vacuolar proton-translocating adenosine triphosphatase

V0 :

domain membrane-integral domain of V-ATPase

V1 :

domain membrane-peripheral domain of V-ATPase

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Authors and Affiliations

  1. Max-Plank-Institut für Züchtungs-forschung, Carl-von-Linné-Weg 10, D-50829, Köln, Federal Republic of Germany

    J. -B. Mariaux

  2. Institut für Botanik, Technische Hochschule Darmstadt, Darmstadt

    E. Fischer-Schliebs, U. Lüttge & R. Ratajczak

Authors
  1. J. -B. Mariaux
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  2. E. Fischer-Schliebs
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  3. U. Lüttge
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  4. R. Ratajczak
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Dedicated to Prof. Dr. Eberhard Schnepf on the occasion of his retirement

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Mariaux, J.B., Fischer-Schliebs, E., Lüttge, U. et al. Dynamics of activity and structure of the tonoplast vacuolar-type H+-ATPase in plants with differing CAM expression and in a C3 plant under salt stress. Protoplasma 196, 181–189 (1997). https://doi.org/10.1007/BF01279566

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  • DOI: https://doi.org/10.1007/BF01279566

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