Aminoacyl-tRNA synthetase-induced cleavage of tRNA

Nucleic Acids Res. 1992 Apr 11;20(7):1523-30. doi: 10.1093/nar/20.7.1523.

Abstract

Aminoacyl-tRNA synthetases interact with their cognate tRNAs in a highly specific fashion. We have examined the phenomenon that upon complex formation E. coli glutaminyl-tRNA synthetase destabilizes tRNA(Gln) causing chain scissions in the presence of Mg2+ ions. The phosphodiester bond cleavage produces 3'-phosphate and 5'-hydroxyl ends. This kind of experiment is useful for detecting conformational changes in tRNA. Our results show that the cleavage is synthetase-specific, that mutant and wild-type tRNA(Gln) species can assume a different conformation, and that modified nucleosides in tRNA enhance the structural stability of the molecule.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acyl-tRNA Synthetases / metabolism*
  • Base Sequence
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Kinetics
  • Magnesium / metabolism
  • Molecular Sequence Data
  • Mutation / genetics
  • Nucleic Acid Conformation
  • RNA, Transfer, Gln / chemistry
  • RNA, Transfer, Gln / metabolism*
  • RNA, Transfer, Trp / chemistry
  • RNA, Transfer, Trp / metabolism

Substances

  • RNA, Transfer, Gln
  • RNA, Transfer, Trp
  • Amino Acyl-tRNA Synthetases
  • glutaminyl-tRNA synthetase
  • Magnesium