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Volume 271, Number 43, Issue of October 25, 1996 pp. 26522-26528
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Characterization of Mutations in the  Subunit of the Mitochondrial F₁-ATPase That Produce Defects in Enzyme Catalysis and Assembly

(Received for publication, July 9, 1996)

From the Department of Surgery and Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan 48201

The ATP2 gene, coding for the  subunit of the mitochondrial F₁-ATPase, was cloned from nine independent isolates of chemically mutagenized yeast. Seven different mutant alleles were identified. In one case the mutation occurs in the mitochondrial targeting sequence (M1I). The remaining six mutations map to the mature part of the  subunit protein and alter amino acids that are conserved in the bovine heart mitochondrial and Escherichia coli  subunit proteins. Biochemical analysis of the yeast atp2 mutants identified two different phenotypes. The G133D, P179L, and G227D mutations correlate with an assembly-defective phenotype that is characterized by the accumulation of the F₁  and  subunits in large protein aggregates. Strains harboring the A192V, E222K, or R293K mutations assemble an F₁ of normal size that is none-the-less catalytically inactive. The effect of the atp2 mutations was also analyzed in diploids formed by crossing the mutants to wild type yeast. Hybrid enzymes formed with  subunits containing either the G133D, E222K, or R293K mutations are compromised for steady-state ATPase activity. The display of partial dominance confirms the importance of Gly¹³³ for structural stability and of Glu²²² and Arg²⁹³ for catalytic cooperativity.

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