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      Environmental study of subunit i, a F(o) component of the yeast ATP synthase.

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          Abstract

          The topology of subunit i, a component of the yeast F(o)F(1)-ATP synthase, was determined by the use of cysteine-substituted mutants. The N(in)-C(out) orientation of this intrinsic subunit was confirmed by chemical modification of unique cysteine residues with 4-acetamido-4'-maleimidylstilbene-2,2'-disulfonic acid. Near-neighbor relationships between subunit i and subunits 6, f, g, and d were demonstrated by cross-link formation following sulfhydryl oxidation or reaction with homobifunctional and heterobifunctional reagents. Our data suggest interactions between the unique membrane-spanning segment of subunit i and the first transmembranous alpha-helix of subunit 6 and a stoichiometry of 1 subunit i per complex. Cross-linked products between mutant subunits i and proteins loosely bound to the F(o)F(1)-ATP synthase suggest that subunit i is located at the periphery of the enzyme and interacts with proteins of the inner mitochondrial membrane that are not involved in the structure of the yeast ATP synthase.

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          Author and article information

          Journal
          Biochemistry
          Biochemistry
          0006-2960
          0006-2960
          Apr 11 2000
          : 39
          : 14
          Affiliations
          [1 ] Institut de Biochimie et Génétique Cellulaires du CNRS, Université Victor Segalen, Bordeaux 2,1 rue Camille Saint-Saëns, 33077 Bordeaux Cedex, France.
          Article
          bi992438l
          10747812
          74a6f583-5934-4790-824d-c74ea2aa9f96
          History

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