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J. Biol. Chem., Vol. 269, Issue 42, 26144-26151, 10, 1994
A Tzagoloff, J Yue, J Jang and MF Paul
Respiration-defective pet mutants of Saccharomyces cerevisiae, assigned to
complementation group G25, are grossly deficient in mitochondrial
respiratory and ATPase complexes. This phenotype is usually found in
strains impaired in mitochondrial protein synthesis. The G25 mutants,
however, synthesize all of the proteins encoded by mitochondrial DNA. The
mutants are also able to import and process cytoplasmically derived
subunits of these enzymes. These results are most compatible with the idea
that the gene defined by G25 mutants (RCA1) codes for a protein essential
for the assembly of functional respiratory and ATPase complexes. The RCA1
gene has been cloned by complementation of an rca1 mutant with a yeast
genomic library. The sequence of the encoded product shows Rca1 protein to
be a new member of a recently described family of ATPases. The Rca1 protein
is a mitochondrial membrane protein and is the third known member of this
family implicated to function in the biogenesis of mitochondria. The
primary structure of Rca1 protein indicates several distinct domains in
addition to the common purine nucleotide binding region shared by all
members of this protein family. One, located in the amino-terminal half,
contains two hydrophobic stretches of sufficient length to span a membrane
lipid bilayer.
A new member of a family of ATPases is essential for assembly of mitochondrial respiratory chain and ATP synthetase complexes in Saccharomyces cerevisiae
Department of Biological Sciences, Columbia University, New York, New York 10027.
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