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- W2023251962 abstract "[32P]tRNALyS, from Escherichia coli, was modified with kethoxal, in the presence and absence of the oligonucleotide codon (A)4. The presence of the codon resulted in a faster modification rate of the tRNA at three guanine sites which were identified by a diagonal fingerprint method. A large increase in the modification rate occurred at the 7-methylguanosine residue 46 (m7G-46) in the presence of the codon; weakly enhanced modification was observed at G-15 and G-57. It is concluded that the formation of a codon-anticodon complex induces, primarily, a confor-mational change involving disruption of the m7G-46 from the m7G-46 · G-22 · C-13 base triple. Subsequently, the guanines of G-15 and G-57, in the D and T loops, respectively, become slightly more reactive, suggesting a weak tendency for these two interacting arms to unfold. The results are interpreted in terms of an equilibrium between two main conformers and a third minor one; the possible significance of these conformers, in protein biosynthesis, is considered." @default.
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- W2023251962 date "1979-07-01" @default.
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- W2023251962 title "Chemical Evidence for a Codon-Induced Allosteric Change in tRNALys Involving the 7-Methylguanosine Residue 46" @default.
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- W2023251962 doi "https://doi.org/10.1111/j.1432-1033.1979.tb13151.x" @default.
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