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Nucleic Acids Research, 1992, Vol. 20, No. 7 1523-1530
© 1992

MOLECULAR BIOLOGY

Aminoacyl-tRNA synthetase-induced cleavage of tRNA

Sergey Beresten, Martina Jahn and Dieter Söll*

Department of Molecular Biophysics and Biochemistry, Yale University PO Box 6666, New Haven, CT 06511, USA

*To whom correspondence should be addressed

Received January 23, 1992. Revised February 28, 1992. Accepted February 28, 1992.

Aminoacyl-tRNA synthetases interact with their cognate tRNAs in a highly specific fashion. We have examined the phenomenon that upon complex formation E. coli glutamlnyl-tRNA synthetase destabilizes tRNAG in 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 tRNAGln species can assume a different conformation, and that modified nucleosides in tRNA enhance the structural stability of the molecule.


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