Journal
FEBS LETTERS
Volume 586, Issue 16, Pages 2232-2238Publisher
WILEY
DOI: 10.1016/j.febslet.2012.05.039
Keywords
Aminoacyl-tRNA synthetase; Archaea; Ribosome; Translation; tRNA
Funding
- National Institutes of Health [GM65183, GM100329-01]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1040302] Funding Source: National Science Foundation
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In archaea and eukaryotes aminoacyl-tRNA synthetases (aaRSs) associate in multi-synthetase complexes (MSCs), however the role of such MSCs in translation is unknown. MSC function was investigated in vivo in the archaeon Thermococcus kodakarensis, wherein six aaRSs were affinity co-purified together with several other factors involved in protein synthesis, suggesting that MSCs may interact directly with translating ribosomes. In support of this hypothesis, the aminoacyl-tRNA synthetase (aaRS) activities of the MSC were enriched in isolated T. kodakarensis polysome fractions. These data indicate that components of the archaeal protein synthesis machinery associate into macromolecular assemblies in vivo and provide the potential to increase translation efficiency by limiting substrate diffusion away from the ribosome, thus facilitating rapid recycling of tRNAs.
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