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Structural basis of specific tRNA aminoacylation by a small in vitro selected ribozyme

Author

Listed:
  • Hong Xiao

    (Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109-1024, USA)

  • Hiroshi Murakami

    (Research Center for Advanced Science and Technology, The University of Tokyo)

  • Hiroaki Suga

    (Research Center for Advanced Science and Technology, The University of Tokyo
    Graduate School of Engineering, The University of Tokyo, 113-8656, Tokyo, Japan)

  • Adrian R. Ferré-D’Amaré

    (Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109-1024, USA)

Abstract

Evolution of protein synthesis During the evolution of protein synthesis in an RNA world, there must have been a stage when RNA acted as a catalyst to add amino acids onto transfer RNAs. Flexizyme is an in vitro evolved ribozyme that specifically adds an amino acid to the terminal 3′-OH of tRNA. Xiao et al. have solved the structure of flexizyme joined to a tRNA mimic. Interestingly, the RNA displays many of the known aminoacyl-tRNA synthetase/tRNA interactions, approaches the tRNA in a similar manner, and adopts an induced fit conformation that enhances specificity.

Suggested Citation

  • Hong Xiao & Hiroshi Murakami & Hiroaki Suga & Adrian R. Ferré-D’Amaré, 2008. "Structural basis of specific tRNA aminoacylation by a small in vitro selected ribozyme," Nature, Nature, vol. 454(7202), pages 358-361, July.
    • Handle: RePEc:nat:nature:v:454:y:2008:i:7202:d:10.1038_nature07033
    DOI: 10.1038/nature07033
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