These authors equally contributed to the work and are listed in alphabetic order.
Mitochondrial translation in absence of local tRNA aminoacylation and methionyl tRNAMet formylation in Apicomplexa
Article first published online: 31 MAR 2010
© 2010 Blackwell Publishing Ltd
Volume 76, Issue 3, pages 706–718, May 2010
How to Cite
Pino, P., Aeby, E., Foth, B. J., Sheiner, L., Soldati, T., Schneider, A. and Soldati-Favre, D. (2010), Mitochondrial translation in absence of local tRNA aminoacylation and methionyl tRNAMet formylation in Apicomplexa. Molecular Microbiology, 76: 706–718. doi: 10.1111/j.1365-2958.2010.07128.x
- Issue published online: 23 APR 2010
- Article first published online: 31 MAR 2010
- Accepted 8 March, 2010.
Apicomplexans possess three translationally active compartments: the cytosol, a single tubular mitochondrion, and a vestigial plastid organelle called apicoplast. Mitochondrion and apicoplast are of bacterial evolutionary origin and therefore depend on a bacterial-like translation machinery. The minimal mitochondrial genome contains only three ORFs, and in Toxoplasma gondii the absence of mitochondrial tRNA genes is compensated for by the import of cytosolic eukaryotic tRNAs. Although all compartments require a complete set of charged tRNAs, the apicomplexan nuclear genomes do not hold sufficient aminoacyl-tRNA synthetase (aaRSs) genes to be targeted individually to each compartment. This study reveals that aaRSs are either cytosolic, apicoplastic or shared between the two compartments by dual targeting but are absent from the mitochondrion. Consequently, tRNAs are very likely imported in their aminoacylated form. Furthermore, the unexpected absence of tRNAMet formyltransferase and peptide deformylase implies that the requirement for a specialized formylmethionyl-tRNAMet for translation initiation is bypassed in the mitochondrion of Apicomplexa.