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Originally published as Genetics Published Articles Ahead of Print on February 3, 2005.
Genetics, Vol. 169, 1891-1901, April 2005, Copyright © 2005
doi:10.1534/genetics.104.037473
Mitochondrial Translation
Elongation Factor Tu Is Essential in Fission Yeast and Depends on an Exchange Factor Conserved in Humans but Not in Budding Yeast
Stéphane Chiron, Audrey Suleau1 and Nathalie Bonnefoy2
Centre de Génétique Moléculaire du CNRS, 91198 Gif-sur-Yvette, France
2 Corresponding author: Centre de Génétique Moléculaire, CNRS Bâtiment 26, 1 Ave. de la Terrasse, 91198 Gif-sur-Yvette Cedex, France.
E-mail: bonnefoy{at}cgm.cnrs-gif.fr
The translation elongation factor EF-Tu is a GTPase that delivers amino-acylated tRNAs to the ribosome during the elongation step of translation. EF-Tu/GDP is recycled by the guanine nucleotide exchange factor EF-Ts. Whereas EF-Ts is lacking in S. cerevisiae, both translation factors are found in S. pombe and H. sapiens mitochondria, consistent with the known similarity between fission yeast and human cell mitochondrial physiology. We constructed yeast mutants lacking these elongation factors. We show that mitochondrial translation is vital for S. pombe, as it is for human cells. In a genetic background allowing the loss of mitochondrial functions, a block in mitochondrial translation in S. pombe leads to a major depletion of mtDNA. The relationships between EF-Ts and EF-Tu from both yeasts and humans were investigated through functional complementation and coexpression experiments and by a search for suppressors of the absence of the S. pombe EF-Ts. We find that S. cerevisiae EF-Tu is functionally equivalent to the S. pombe EF-Tu/EF-Ts couple. Point mutations in the S. pombe EF-Tu can render it independent of its exchange factor, thereby mimicking the situation in S. cerevisiae.
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