- THIS ARTICLE
- Full Text (PDF)
- Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Folley, L. S.
- Articles by Fox, T. D.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Folley, L. S.
- Articles by Fox, T. D.
Genetics, Vol 129, 659-668, Copyright © 1991
INVESTIGATIONS |
Site-Directed Mutagenesis of a Saccharomyces cerevisiae Mitochondrial Translation Initiation Codon
L. S. Folley and T. D. Fox
Section of Genetics and Development, Cornell University, Ithaca, New York 14853-2703
We have used a generally applicable strategy for gene replacement in yeast mitochondria to mutate the translation initiation codon of the COX3 gene from AUG to AUA. The mutation, cox3-1, substantially reduced, but did not eliminate, translation of cytochrome c oxidase subunit III (coxIII). Strains bearing the mutation exhibited a leaky (partial) nonrespiratory growth phenotype and a reduced incorporation of radiolabeled amino acids into coxIII in vivo in the presence of cycloheximide. Hybridization experiments demonstrated that the mutation had little or no effect on levels of the COX3 mRNA. Residual translation of the cox3-1 mutant mRNA was dependent upon the three nuclearly coded mRNA-specific activators PET494, PET54 and PET122, known from previous studies to work through a site (or sites) upstream of the initiation codon to promote translation of the wild-type mRNA. Furthermore, respiratory growth of cox3-1 mutant strains was sensitive to decreased dosage of genes PET494 and PET122 in heterozygous mutant diploids, unlike the growth of strains carrying wild-type mtDNA. Some residual translation of the cox3-1 mRNA appeared to initiate at the mutant AUA codon, despite the fact that the 610-base 5'-mRNA leader contains numerous AUA triplets. We conclude that, while AUG is an important component of the COX3 translation initiation site, the site probably is also specified by other sequence or structural features.
This article has been cited by other articles:
 |
|
 |
|
  E. H. Williams, C. A. Butler, N. Bonnefoy, and T. D. Fox Translation Initiation in Saccharomyces cerevisiae Mitochondria: Functional Interactions Among Mitochondrial Ribosomal Protein Rsm28p, Initiation Factor 2, Methionyl-tRNA-Formyltransferase and Novel Protein Rmd9p Genetics, March 1, 2007; 175(3): 1117 - 1126. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. H. Williams, N. Bsat, N. Bonnefoy, C. A. Butler, and T. D. Fox Alteration of a Novel Dispensable Mitochondrial Ribosomal Small-Subunit Protein, Rsm28p, Allows Translation of Defective COX2 mRNAs Eukaryot. Cell, February 1, 2005; 4(2): 337 - 345. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Bonnefoy, N. Bsat, and T. D. Fox Mitochondrial Translation of Saccharomyces cerevisiae COX2 mRNA Is Controlled by the Nucleotide Sequence Specifying the Pre-Cox2p Leader Peptide Mol. Cell. Biol., April 1, 2001; 21(7): 2359 - 2372. [Abstract] [Full Text]
|
|
|
|
 |
|
 J. E. G. McCarthy Posttranscriptional Control of Gene Expression in Yeast Microbiol. Mol. Biol. Rev., December 1, 1998; 62(4): 1492 - 1553. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. S. Green-Willms, T. D. Fox, and M. C. Costanzo Functional Interactions between Yeast Mitochondrial Ribosomes and mRNA 5' Untranslated Leaders Mol. Cell. Biol., April 1, 1998; 18(4): 1826 - 1834. [Abstract] [Full Text]
|
|
|
|
 |
|
 J Nunnari, T. Fox, and P Walter A mitochondrial protease with two catalytic subunits of nonoverlapping specificities Science, December 24, 1993; 262(5142): 1997 - 2004. [Abstract] [PDF]
|
|