Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex.

@article{Hausmann2008StructuralAF,
  title={Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex.},
  author={Corinne D. Hausmann and Michael Ibba},
  journal={FEBS letters},
  year={2008},
  volume={582 15},
  pages={2178-82}
}
Methanothermobacter thermautotrophicus contains a multi-aminoacyl-tRNA synthetase complex (MSC) of LysRS, LeuRS and ProRS. Elongation factor (EF) 1A also associates to the MSC, with LeuRS possibly acting as a core protein. Analysis of the MSC revealed that LysRS and ProRS specifically interact with the idiosyncratic N- and C- termini of LeuRS, respectively. EF-1A instead interacts with the inserted CP1 proofreading domain, consistent with models for post-transfer editing by class I synthetases… CONTINUE READING

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