AMINOACYL-TRANSFER-RNA SYNTHETASES FROM BAKERS-YEAST - REACTING SITE OF ENZYMATIC AMINOACYLATION IS NOT UNIFORM FOR ALL TRANSFER-RNA
AMINOACYL-TRANSFER-RNA SYNTHETASES FROM BAKERS-YEAST - REACTING SITE OF ENZYMATIC AMINOACYLATION IS NOT UNIFORM FOR ALL TRANSFER-RNA
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DOI:
10.1016/0014-5793(75)81093-3
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发表时间:
1975-01-01
期刊:
影响因子:
3.5
通讯作者:
STERNBACH, H
中科院分区:
文献类型:
--
作者:
CRAMER, F;FAULHAMMER, H;STERNBACH, H
In previous work we showed that tRNAPhe from baker’s yeast was phenylalanylated exclusively at the 2’hydroxyl group of the terminal ribose by phenylalanyl-tRNA synthetase [1, 2]. This was based on the observation that after incorporation of 3’deoxyadenosine and 2’deoxyadenosine, respectively, into the terminus of tRNAPhe only tRNAPhe-CC-3’dA could be aminoacylated whereas tRNAPhe-CC-2’dA was a competitive inhibitor of the enzyme. The same result was later obtained, by an independent method, for tRNAPhe from Escherichiu coli and from rat liver [3]. These results seemed to be reasonable also from the chemical point of view as suggested by Zamecnik [4] since the 2’hydroxyl group is generally more reactive towards acylation. We then tested tRNAne, tRNASeT*, tRNATvr, and tRNAVa’from yeast in order to check the general validity of the enzymatic aminoacylation of the more reactive 2’hydroxyl group. We found, however, three classes of tRNAs: those aminoacylated at the 2’hydroxyl group, those aminoacylated at the 3’hydroxyl group and those aminoacylatable at both hydroxyl groups.