Aminoacyl-tRNA synthetase-induced cleavage of tRNA
Copyright policy )Aminoacyl-tRNA synthetase-induced cleavage of tRNA
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.
- Yale University United States
Amino Acyl-tRNA Synthetases, Kinetics, Base Sequence, RNA, Transfer, Gln, Molecular Sequence Data, Mutation, Escherichia coli, Nucleic Acid Conformation, Magnesium, RNA, Transfer, Trp
Amino Acyl-tRNA Synthetases, Kinetics, Base Sequence, RNA, Transfer, Gln, Molecular Sequence Data, Mutation, Escherichia coli, Nucleic Acid Conformation, Magnesium, RNA, Transfer, Trp
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