Comparative X-ray structure analysis of human and Escherichia coli tRNA(Gly) acceptor stem microhelices

Biochem Biophys Res Commun. 2008 Apr 18;368(4):1002-6. doi: 10.1016/j.bbrc.2008.01.174. Epub 2008 Feb 12.

Abstract

tRNA identity elements assure the correct aminoacylation of tRNAs by the aminoacyl-tRNA synthetases with the cognate amino acid. The tRNA(Gly)/glycyl-tRNA sythetase system is member of the so-called 'class II system' in which the tRNA determinants consist of rather simple elements. These are mostly located in the tRNA acceptor stem and in the glycine case additionally the discriminator base at position 73 is required. Within the glycine-tRNA synthetases, the archaebacterial/human and the eubacterial sytems differ with respect to their protein structures and the required tRNA identity elements, suggesting a unique evolutionary divergence. In this study, we present a comparison between the crystal structures of the eubacterial Escherichia coli and the human tRNA(Gly) acceptor stem microhelices and their surrounding hydration patterns.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Escherichia coli / genetics*
  • Glycine-tRNA Ligase / chemistry*
  • Humans
  • Models, Molecular
  • Nucleic Acid Conformation
  • RNA, Transfer, Gly / chemistry*
  • Water / chemistry

Substances

  • RNA, Transfer, Gly
  • Water
  • Glycine-tRNA Ligase