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A more recent version of this article appeared on January 1, 2003
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Submitted on August 13, 2002
Accepted on September 20, 2002
1 Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853-2703
* Corresponding author. E-mail address: tdf1{at}cornell.edu.
The core of the cytochrome c oxidase complex is composed of its three largest subunits, Cox1p, Cox2p and Cox3p, which are encoded in mitochondrial DNA of S. cerevisiae and inserted into the inner membrane from the inside. Mitochondrial translation of the COX1, COX2, and COX3 mRNAs is activated mRNA-specifically by the nuclearly coded proteins Pet309p, Pet111p, and the concerted action of Pet54p, Pet122p and Pet494p, respectively. Since the translational activators recognize sites in the 5'-untranslated leaders of these mRNAs, and since untranslated mRNA sequences contain information for targeting their protein products, the activators are likely to play a role in localizing translation. Here, we report physical associations among the mRNA-specific translational activator proteins, located on the matrix side of the inner membrane. These interactions, detected by coimmune precipitation and by two-hybrid experiments, suggest that the translational activator proteins could be organized on the surface of the inner membrane such that synthesis of Cox1p, Cox2p and Cox3p would be co-localized in a way that facilitates assembly of the core of the cytochrome c oxidase complex. In addition, we found interactions between Nam1p/Mtf2p and the translational activators, suggesting an organized delivery of mitochondrial mRNAs to the translation system.
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