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J. Biol. Chem., Vol. 260, Issue 3, 1513-1520, Feb, 1985
CL Dieckmann and A Tzagoloff
A new gene function involved in the expression of mitochondrial cytochrome
b is described. E158 is a respiratory deficient strain of Saccharomyces
cerevisiae with a recessive mutation in nuclear DNA. The block in
mitochondrial respiration is a consequence of the mutant's inability to
synthesize cytochrome b. This has been confirmed by analysis of the
mitochondrial translation products in E158. Since the mutant has wild-type
concentrations of mature cytochrome b mRNA, the absence of the cytochrome b
protein cannot be due to a transcriptional or RNA-processing defect. The
wild-type gene (CBP6) responsible for the observed phenotype has been
cloned by transformation of E158 with a genomic library of yeast nuclear
DNA. The cloned gene has been sequenced and shown to code for a basic
protein with a molecular weight of 18,657. Both deletion and disruption of
the CBP6 coding sequence in chromosomal DNA of wild-type yeast lead to
respiratory deficiency with a concomitant loss of cytochrome b. Part of the
CBP6 gene has been fused to the trpE gene on a high expression Escherichia
coli vector. The hybrid protein encoded by the trpE/CBP6 fusion has been
purified from E. coli and used as an antigen for antibody production.
Antibodies to the hybrid protein cross-react with an 18-kDa protein present
in yeast mitochondria.
Assembly of the mitochondrial membrane system. CBP6, a yeast nuclear gene necessary for synthesis of cytochrome b
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