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J Biol Chem, Vol. 274, Issue 1, 543-548, January 1, 1999
From the Institut de Biochimie et Génétique Cellulaires
du CNRS, Université Victor Ségalen, Bordeaux 2, 33077 Bordeaux cedex, France
Two subunits of the yeast ATP synthase have been
isolated. Subunit e was found loosely associated to the complex. Triton
X-100 at a 1% concentration removed this subunit from the ATP
synthase. The N-terminal sequencing of subunit i has been performed.
The data are in agreement with the sequence of the predicted product of
a DNA fragment of Saccharomyces cerevisiae chromosome XIII. The ATP18 gene encodes subunit i, which is 59 amino acids
long and corresponds to a calculated mass of 6687 Da. Its pI is 9.73. It is an amphiphilic protein having a hydrophobic N-terminal part and a
hydrophilic C-terminal part. It is not apparently related to any
subunit described in other ATP synthases. The null mutant showed low
growth on nonfermentable medium. Mutant mitochondria display a low
ADP/O ratio and a decrease with time in proton pumping after ATP
addition. Subunit i is associated with the complex; it is not a
structural component of the enzyme but rather is involved in the
oxidative phosphorylations. Similar amounts of ATP synthase were
measured for wild-type and null mutant mitochondria. Because 2-fold
less specific ATPase activity was measured for the null mutant than for
the wild-type mitochondria, we make the hypothesis that the observed
decrease in the turnover of the mutant enzyme could be linked to a
proton translocation defect through F0.
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