The effect of specific structural modification on the biological activity of E.coli arginine tRNA
- 1 March 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 5 (3), 879-892
- https://doi.org/10.1093/nar/5.3.879
Abstract
Escherichia coli arginine tRNA 1 has been modified at position s 2 C32 with iodoacetamide and a spin labelled derivative. The small effects on the charging ability of tRNA by the modifications suggest that the synthetase does not bind to the tRNA in this region of the anticodon loop before the anticodon. A ternary complex of elongation factor Tu, GTP and the modified Arg-tRNA, can be formed allowing future studies of enzymatic binding to the ribosome. Using the triplet binding assay the native Arg-tRNA 1 decodes all 4 codons beginning with CG. The modified Arg-tRNA 1 has a restricted decoding but the decoding pattern is still unusual according to the Wobblε Hypothesis.Keywords
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