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J Biol Chem, Vol. 275, Issue 20, 14898-14902, May 19, 2000
From the Nuclear mutants of Saccharomyces
cerevisiae assigned to complementation group G34 are
respiratory-deficient and lack cytochrome oxidase activity and the
characteristic spectral peaks of cytochromes a and
a3. The corresponding gene was cloned by
complementation, sequenced, and identified as reading frame YGR062C on
chromosome VII. This gene was named COX18. The
COX18 gene product is a polypeptide of 316 amino acids with
a putative amino-terminal mitochondrial targeting sequence and
predicted transmembrane domains. Respiratory chain carriers other than
cytochromes a and a3 and the ATPase complex are present at near wild-type levels in cox18
mutants, indicating that the mutations specifically affect cytochrome
oxidase. The synthesis of Cox1p and Cox3p in mutant mitochondria is
normal whereas Cox2p is barely detected among labeled mitochondrial
polypeptides. Transcription of COX2 does not require
COX18 function, and a chimeric COX3-COX2 mRNA did not suppress the
respiratory defect in the null mutant, indicating that the mutation
does not impair transcription or translation of the mRNA. Western
analysis of cytochrome oxidase subunits shows that inactivation of the
COX18 gene greatly reduces the steady state amounts of
subunit 2 and results in variable decreases in other subunits of
cytochrome oxidase. A gene fusion expressing a biotinylated form of
Cox18p complements cox18 mutants. Biotinylated Cox18p is a
mitochondrial integral membrane protein. These results indicate Cox18p
to be a new member of a group of mitochondrial proteins that function
at a late stage of the cytochrome oxidase assembly pathway.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) U59742.
Cloning and Characterization of COX18, a
Saccharomyces cerevisiae PET Gene Required for the Assembly
of Cytochrome Oxidase*
,
**
Departamento de Microbiologia, Instituto de
Ciências Biomédicas, Universidade de São Paulo, Av.
Prof. Lineu Prestes, 1374, 05508-900, São Paulo, SP, Brazil, the
§ Department of Molecular Biology and Genetics, Cornell
University, Ithaca, New York 14853-2703, the ¶ Department of
Biological Sciences, Columbia University, New York, New York 10027, and
the Instituto de Pesquisa e Desenvolvimento, Universidade do
Vale do Paraíba, Av. Shishima Hifumi, 2911, 12244-000 São José dos Campos, SP, Brazil
*
This research was partially supported by grants from the
Conselho Nacional de Desenvolvimento Científico e
Tecnológico and Fundação de Amparo à Pesquisa
do Estado de São Paulo (to F. G. N.), by National Institutes of
Health Training Grant GM07617 and Research Grant GM29362 (to
T. D. F.), and by National Institutes of Health Research Grant
GM50187 (to A. T.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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