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MBC in Press, published online ahead of print November 29, 2006
Mol. Biol. Cell 10.1091/mbc.E06-09-0803

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Submitted on September 8, 2006
Revised on November 3, 2006
Accepted on November 20, 2006

Aberrant Translation of Cytochrome c Oxidase Subunit 1 mRNA Species in the Absence of Mss51p in the Yeast Saccharomyces cerevisiae

Andrea Zambrano,* Flavia Fontanesi,* Asun Solans,* Rodrigo Leite de Oliveira,* Thomas D. Fox,{dagger} Alexander Tzagoloff,{ddagger} and Antoni Barrientos*

*Department of Neurology and Biochemistry and Molecular Biology, The John T. Macdonald Foundation Center for Medical Genetics, University of Miami School of Medicine, Miami, FL 33136; {dagger}Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853-2703; {ddagger}Department of Biological Sciences, Columbia University, New York, NY 10027

Monitoring Editor: Peter Walter

Expression of yeast mitochondrial genes depends on specific translational activators acting on the 5'-untranslated region of their target mRNAs. Mss51p is a translational factor for cytochrome c oxidase subunit 1 (COX1) mRNA and a key player in down-regulating Cox1p expression when subunits with which it normally interacts are not available. Mss51p probably acts on the 5'-untranslated region of COX1 mRNA to initiate translation and on the coding sequence itself to facilitate elongation. Mss51p binds newly synthesized Cox1p, an interaction that could be necessary for translation. To gain insight into the different roles of Mss51p on Cox1p biogenesis we have analyzed the properties of a new mitochondrial protein, mp15, which is synthesized in mss51 mutants and in cytochrome oxidase mutants in which Cox1p translation is suppressed. The mp15 polypeptide is not detected in cox14 mutants that express Cox1p normally. We show that mp15 is a truncated translation product of COX1 mRNA which synthesis requires the COX1 mRNA specific translational activator Pet309p. These results support a key role for Mss51p in translationally regulating Cox1p synthesis by the status of cytochrome oxidase assembly.

Address correspondence to: Antoni Barrientos (abarrientos{at}med.miami.edu)




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