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

Hong Xiao, Hiroshi Murakami, Hiroaki Suga and Adrian R. Ferré-D’Amaré ()
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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
Adrian R. Ferré-D’Amaré: Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, Washington 98109-1024, USA

Nature, 2008, vol. 454, issue 7202, 358-361

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.

Date: 2008
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DOI: 10.1038/nature07033

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