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.
Beresten
S
S
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
Jahn
M
M
Söll
D
D
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D009690:Nucleic Acid Conformation; D012351:RNA, Transfer, Gln / Q000737:chemistry / Q000378:metabolism*; D012364:RNA, Transfer, Trp / Q000737:chemistry / Q000378:metabolism
D012351:RNA, Transfer, Gln; D012364:RNA, Transfer, Trp; D000604:Amino Acyl-tRNA Synthetases; C020659:glutaminyl-tRNA synthetase; D008274:Magnesium