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Originally published as MBC in Press, 10.1091/mbc.E06-09-0803 on November 29, 2006

Vol. 18, Issue 2, 523-535, February 2007

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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{dagger}, Thomas D. Fox{ddagger}, Alexander Tzagoloff§, 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}Life and Health Sciences Research Institute (ICVS), Health Sciences School, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal; {ddagger}Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853-2703; and §Department of Biological Sciences, Columbia University, New York, NY 10027

Submitted September 8, 2006; Revised November 3, 2006; Accepted November 20, 2006
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 whose 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.


This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-09-0803) on November 29, 2006.

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

Abbreviations used: CAP, chloramphenicol; COX, cytochrome c oxidase; GST, glutathione S-transferase; UTR, untranslated region; Y3H, yeast three-hybrid system.




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