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A more recent version of this article appeared on February 1, 2007
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Submitted on September 15, 2006
Revised on November 3, 2006
Accepted on November 7, 2006
*Laboratoire de Génétique Moléculaire, Centre National de la Recherche Scientifique-Ecole Normale Supérieur, and
Plateforme Transcriptome IFR36, Ecole Normale Supérieure, 75230 Paris Cedex 05;
Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461
Monitoring Editor: Thomas Fox
The coherence of mitochondrial biogenesis relies on spatiotemporally coordinated associations of 800-1000 proteins mostly encoded in the nuclear genome. We report the development of new quantitative analyses to assess the role of local protein translation in the construction of molecular complexes. We used real time PCR to determine the cellular location of 112 mRNAs involved in seven mitochondrial complexes. Five typical cases were examined by an improved FISH protocol. The proteins produced in the vicinity of mitochondria (MLR proteins) were, almost exclusively, of prokaryotic origin, and are key elements of the core construction of the molecular complexes; the accessory proteins were translated on free cytoplasmic polysomes. These two classes of proteins correspond, at least as far as intermembrane space (IMS) proteins are concerned, to two different import pathways. Import of MLR proteins involves both TOM and TIM23 complexes whereas nonMLR proteins only interact with the TOM complex. Site-specific translation loci, both outside and inside mitochondria, may coordinate the construction of molecular complexes composed of both nuclearly and mitochondrially encoded subunits.
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