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- W2092289968 abstract "Abstract The structure of the complex of Ile-tRNA synthetase and tRNA Ile has been studied by subjecting the free and bound nucleic acid to attack by specific nucleases. It was found that the anticodon region, which is quickly cut in free tRNA Ile by ribonucleases A and T1, is protected from attack in the synthetase-tRNA complex. In addition, cleavage at the 3′-terminus of the tRNA is inhibited by the bound protein. These results confirm by an independent method studies which showed that in the complex both the anticodon and 3′-terminus are blocked from oligonucleotide hybridization (Schimmel, P. R., Uhlenbeck, O. C., Lewis, J. B., Dickson, L. A., Eldred, E. W. and Schreier, A. A. (1972) Biochemistry 11, 642–646). Noncognate interactions were also explored. These included Tyr-tRNA synthetase with tRNA Ile and Ile-tRNA synthetase with tRNA Tyr Although no strong interaction was detected in the latter case, the former shows significant complex formation. This “incorrect” complex of tyrosyl-tRNA synthetase and tRNA Ile is protected from nuclease attack in a similar way as observed for the cognate complex. This suggests that the orientation of the noncognate enzyme on tRNA Ile is like that of the cognate enzyme." @default.
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- W2092289968 date "1975-04-01" @default.
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- W2092289968 title "Structure of transfer RNA—Aminoacyl transfer RNA synthetase complexes investigated by nuclease digestion" @default.
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- W2092289968 doi "https://doi.org/10.1016/0003-9861(75)90507-x" @default.
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