RECOVERY OF TYROSINE ACCEPTOR ACTIVITY BY COMBINING 3'-HALF MOLECULE WITH STEPWISE DEGRADATION PRODUCTS OF 5'-HALF MOLECULE OBTAINED FROM TYROSINE TRNA

Two half molecules were obtained from purified Torulopsis utilis tyrosine tRNA by scission with RNase T1 of the G-ψ bond of the presumed anticodon GψA. When these halves were mixed, full tyrosine acceptor activity was recovered, although each of the halves was inactive. After splitting the 3′-terminal residues of the 5′-half and mixing the products with the 3′-half, the activity was fully recovered as compared with native tyrosine tRNA, clearly indicating that the first letter of the anticodon is not regarded as one of the tyrosine recognition sites. © 1969.