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Ion-translocating ATPases in tendrils ofBryonia dioica Jacq.

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Abstract

Procedures have been developed which allow the preparation of highly pure endoplasmic reticulum and plasma membrane from tendrils ofBryonia dioica. These and further membrane fractions were used to study vanadate-sensitive ATPase activity as well as Mg2+ATP-driven transport of45Ca2+. Calcium-translocating ATPases were detected in the endoplasmic reticulum, the plasma membrane and the mitochondrial fraction and characterized kinetically and with respect to the effects of various inhibitors. The endoplasmic-reticulum Ca2+-translocating ATPase was stimulated by KCl and was calmodulin-dependent. The plasma-membrane enzyme was not affected by these agents. These, as well as the inhibitor data, show that the Ca2+-translocating ATPases of the endoplasmic reticulum and the plasma membrane are distinctly different enzymes. Upon mechanical stimulation, the activities of the vanadate-sensitive K+, Mg2+-ATPase and the Ca2+-translocating ATPase(s) increased rapidly and transiently, indicating that increasing transmembrane proton and calcium fluxes are involved in the early stages of tendril coiling.

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Abbreviations

CAM:

calmodulin

CCCP:

carbonylcyanidem-chlorophenylhydrazone

IC50 :

concentration giving 50% inhibition

PM:

plasma membrane

rER:

rough endoplasmic reticulum

sER:

smooth endoplasmic reticulum

FC:

fusicoccin

U3+U3 :

the two PM-rich upper phases obtained after phase partitioning of microsomal membranes

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Authors and Affiliations

  1. Lehrstuhl für Pflanzenphysiologie, Ruhr-Universität, D-44780, Bochum, Germany

    H. Liß & E. W. Weiler

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  1. H. Liß
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  2. E. W. Weiler
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The authors wish to thank the Deutsche Forschungsgemeinschaft, Bonn, Germany, and the Fonds der Chemischen Industrie, Frankfurt, Germany (literature provision) for financial support.

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Liß, H., Weiler, E.W. Ion-translocating ATPases in tendrils ofBryonia dioica Jacq.. Planta 194, 169–180 (1994). https://doi.org/10.1007/BF01101675

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  • DOI: https://doi.org/10.1007/BF01101675

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