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Subunit f of the Yeast Mitochondrial ATP Synthase: Topological and Functional Studies

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Abstract

Modified versions of subunit f were produced by mutagenesis of theATP17 gene of Saccharomyces cerevisiae. A version of subunit f devoid of thelast 28 amino acid residues including the unique transmembranous domaincomplemented the oxidative phosphorylation of the null mutant. However, atwo-fold decrease in the specific ATP synthase activity was measured andattributed to a decrease in the stability of the mutant ATP synthase complexas shown by the low oligomycin-sensitive ATPase activity at alkaline pH. Themodification or not by non-permeant maleimide reagents of cysteine residuesintroduced at the N and C termini of subunit f indicated aNin-Cout orientation. From the C terminus of subunit fit was possible to cross-link subunit 4 (also called subunit b), which isanother component of the F0 sector and which also displays a shorthydrophilic segment exposed to the intermembrane space.

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Authors and Affiliations

  1. Institut de Biochimie et Génétique Cellulaires du CNRS, Université Victor Séalen, Bordeaux2 1 rue Camile Saint Saëns, 33077, Bordeaux dedex, France

    Stéphane Roudeau, Christelle Spannagel, Jacques Vaillier, Geneviève Arselin, Pierre-Vincent Graves & Jean Velours

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  1. Stéphane Roudeau
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  2. Christelle Spannagel
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  3. Jacques Vaillier
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  4. Geneviève Arselin
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  5. Pierre-Vincent Graves
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  6. Jean Velours
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Roudeau, S., Spannagel, C., Vaillier, J. et al. Subunit f of the Yeast Mitochondrial ATP Synthase: Topological and Functional Studies. J Bioenerg Biomembr 31, 85–94 (1999). https://doi.org/10.1023/A:1005407525915

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