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Threonyl‐tRNA synthetase from yeast Aminoacylation of tRNA on its non‐accepting 3′‐terminal hydroxyl group and its behaviour in enzyme‐catalyzed deacylation
Author(s) -
Igloi Gabor L.,
Cramer Friedrich
Publication year - 1978
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(78)80306-8
Subject(s) - aminoacylation , transfer rna , enzyme , hydrolysis , chemistry , yeast , biochemistry , amino acid , catalysis , salt (chemistry) , stereochemistry , rna , organic chemistry , gene
Methods have been developed by which tRNA Thr may be aminoacylated at the normally non–accepting 3’–terminal ribose OH. Two of the methods utilize the mischarging ability of the synthetases under special conditions of low salt concentration and presence of organic solvents. The third method demonstrates for the first time that for some synthetases the 2’,3’ specificity may be manipulated by use of similar special conditions. In the case of threonyl–tRNA synthetase, Thr–tRNA Thr –C–C–A(3’d) has been synthesised by this method. The behaviour of threonyl esters of tRNA Thr –C–C–A, tRNA Thr –C–C–A(2’d) and tRNA Thr –C–C–A(3’d) in the free enzyme–catalyzed deacylation has been studied and the results indicate that the cis diol functional group is necessary for this hydrolysis. The position on the terminal ribose from which the amino acid is removed in this reaction remains to be identified.