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Activation and Deactivation of F0F1-ATPase in Yeast Mitochrondia

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Abstract

The regulation of membrane-bound proton F0F1ATPase by the protonmotive force and nucleotides was studied in yeastmitochondria. Activation occurred in whole mitochondria and the ATPaseactivity was measured just after disrupting the membranes with Triton X-100.Deactivation occurred either in whole mitochondria uncoupled with FCCP, or indisrupted membranes. No effect of Triton X-100 on the ATPase was observed,except a slow reactivation observed only in the absence of MgADP. BothAMPPNP and ATP increased the ATPase deactivation rate, thus indicating thatoccupancy of nucleotidic sites by ATP is more decisive than catalyticturnover for this process. ADP was found to stimulate the energy-dependentATPase activation. ATPase deactivated at the same rate in uncoupled anddisrupted mitochondria. This suggests that deactivation is not controlled byrebinding of some soluble factor, like IF1, but rather by the conversion ofthe F1.IF1 complex into an inactive form.

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Authors and Affiliations

  1. Section de Bioenergetique, CEA Saclay, F91191, Gif-sur-Yvette Cedex, France

    Christelle Schouppe & Francis Haraux

  2. Institute of Biochemie et de Genetique Cellulaires, UPR 9026, CNRS-Universite Bordeaux 2, F33077, Bordeaux Cedex, France

    Jacques Vaillier, Michel Rigoulet & Jean Velours

  3. Proteines Membranaires Transductrices d'Energie, URA 2096, CNRS-CEA Saclay, F91191, Gifsur-Yvette Cedex, France

    Renée Venard & Francis Haraux

Authors
  1. Christelle Schouppe
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  2. Jacques Vaillier
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  3. Renée Venard
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  4. Michel Rigoulet
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  5. Jean Velours
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  6. Francis Haraux
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Schouppe, C., Vaillier, J., Venard, R. et al. Activation and Deactivation of F0F1-ATPase in Yeast Mitochrondia. J Bioenerg Biomembr 31, 105–117 (1999). https://doi.org/10.1023/A:1005495626823

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