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

Aminoacyl-tRNA synthetase-induced cleavage of tRNA

S Beresten  1 , M Jahn, D Söll
Affiliations
Free PMC article

Aminoacyl-tRNA synthetase-induced cleavage of tRNA

S Beresten et al. Nucleic Acids Res. .
Free PMC article

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.

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