Abstract
The biological activity of 335 nm irradiated tRNA Val containing a covalent bond between the 4tU in position 8 and the C in position 13 was tested. The irradiated tRNA is fully acylated but its affinity for the synthetase is decreased by a factor of three as revealed by competition experiments. On the contrary, no difference was observed between normal and irradiated tRNA for ribosome binding in the presence of poly (U,G). Furthermore, the valine acylated to irradiated tRNA was incorporated into polypeptide chains with a rate that was twofold slower than with normal tRNA. These results show that the 4tU-C region can influence the synthetase binding and that tRNA function does not require large spatial separation of bases in this region.
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