Import of tRNAs and aminoacyl-tRNA synthetases into mitochondria

Duchêne, Anne‐Marie; Pujol, Claire; Maréchal-Drouard, Laurence

doi:10.1007/s00294-008-0223-9

Cited by 130 publications

(108 citation statements)

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“…Several reasons can explain this extensive variation: increase can be due to changes in the genetic code or a consequence of tRNA gene duplication, while decrease is generally due to the loss of mt tRNA genes during evolution, compensated by the import of nucleus-encoded tRNAs, a classical phenomenon in mitochondria. 12,13 Alternatively, variation in tRNA gene number in annotated genomes may also be the consequence of defects of tRNA search algorithms that identify false positive tRNA or conversely fail to detect them. Metazoan mt tRNAs often appear degenerated, without the complete cloverleaf secondary structure: absence of the highly conserved D-loop and/or T-loop and even complete arms renders their detection problematic.…”

Section: Introductionmentioning

confidence: 99%

Large gene overlaps and tRNA processing in the compact mitochondrial genome of the crustaceanArmadillidium vulgare

et al. 2015

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Section: Introductionmentioning

confidence: 99%

Large gene overlaps and tRNA processing in the compact mitochondrial genome of the crustaceanArmadillidium vulgare

et al. 2015

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“…It was characterized in a variety of species, and apparently unrelated molecular mechanisms have been discovered for protozoa, higher plants, and yeast (for review, see Tarassov et al 2007;Salinas et al 2008;Duchene et al 2009). In the yeast Saccharomyces cerevisiae, cytosolic tRNA Lys CUU (hereafter referred to as tRK1) is partially targeted into mitochondria (Martin et al 1977).…”

Section: Introductionmentioning

confidence: 99%

Selection of RNA aptamers imported into yeast and human mitochondria

Kolesnikova¹,

Kazakova²,

Comte³

et al. 2010

RNA

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In the yeast Saccharomyces cerevisiae, nuclear DNA-encoded tRNA Lys CUU is partially imported into mitochondria. We previously found that the synthetic transcripts of yeast tRNA Lys and a number of their mutant versions could be specifically internalized by isolated yeast and human mitochondria. The mitochondrial targeting of tRNA Lys in yeast was shown to depend on the cytosolic precursor of mitochondrial lysyl-tRNA synthetase and the glycolytic enzyme enolase. Here we applied the approach of in vitro selection (SELEX) to broaden the spectrum of importable tRNA-derived molecules. We found that RNAs selected for their import into isolated yeast mitochondria have lost the potential to acquire a classical tRNA-shape. Analysis of conformational rearrangements in the importable RNAs by in-gel fluorescence resonance energy transfer (FRET) approach permitted us to suggest that protein factor binding and subsequent import require formation of an alternative structure, different from a classic L-form tRNA model. We show that in the complex with targeting protein factor, enolase 2, tRK1 adopts a particular conformation characterized by bringing together the 39-end and the TCC loop. This is a first evidence for implication of RNA secondary structure rearrangement in the mechanism of mitochondrial import selectivity. Based on these data, a set of small RNA molecules with significantly improved efficiency of import into yeast and human mitochondria was constructed, opening the possibility of creating a new mitochondrial vector system able to target therapeutic oligoribonucleotides into deficient human mitochondria.

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“…In most eukaryotic species mitochondria and chloroplasts contain a full or almost full complement of tRNAs that are exclusively used by the translation machinery of the organelle (11). It is unclear why all eukaryotic cells maintain separate translational apparatuses for the cytosol and the mitochondria.…”

mentioning

confidence: 99%

A mechanism for functional segregation of mitochondrial and cytosolic genetic codes

Español

Thut

Schneider

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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The coexistence of multiple gene translation machineries is a feature of eukaryotic cells and a result of the endosymbiotic events that gave rise to mitochondria, plastids, and other organelles. The conditions required for the integration of these apparatuses within a single cell are not understood, but current evidence indicates that complete ablation of the mitochondrial protein synthesis apparatus and its substitution by its cytosolic equivalent is not possible. Why certain mitochondrial components and not others can be substituted by cytosolic equivalents is not known. In trypanosomatids this situation reaches a limit, because certain aminoacyl-tRNA synthetases are mitochondrial specific despite the fact that all tRNAs in these organisms are shared between cytosol and mitochondria. Here we report that a mitochondria-specific lysyl-tRNA synthetase in Trypanosoma has evolved a mechanism to block the activity of the enzyme during its synthesis and translocation. Only when the enzyme reaches the mitochondria is it activated through the cleavage of a C-terminal structural extension, preventing the possibility of the enzyme being active in the cytosol.aminoacyl-tRNA synthetases ͉ mitochondria ͉ tRNA ͉ trypanosoma

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Import of tRNAs and aminoacyl-tRNA synthetases into mitochondria

Cited by 130 publications

References 110 publications

Large gene overlaps and tRNA processing in the compact mitochondrial genome of the crustaceanArmadillidium vulgare

Large gene overlaps and tRNA processing in the compact mitochondrial genome of the crustaceanArmadillidium vulgare

Selection of RNA aptamers imported into yeast and human mitochondria

A mechanism for functional segregation of mitochondrial and cytosolic genetic codes

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