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Effect of ribothymidine in specific eukaryotic tRNAs on their efficiency in in vitro protein synthesis

Nature volume 261, pages 159–162 (1976)Cite this article

Abstract

RIBOTHYMIDINE (m5U or rT), the most common methylated nucleoside found in tRNA, is always at the 23rd position from the 3′ end in the nucleotide sequence GTψCPurine1,2. So far ribothymidine has been found in essentially all pro-karyotic tRNAs which function in protein synthesis, but not in several eukaryotic ‘elongator’ tRNAs3–6. In the case of wheat germ, all the glycine tRNAs, several species of threonine tRNA and one species of tyrosine tRNA have an unmodified uridine in the position usually occupied by ribothymidine (ref. 5 and K.B.M., D. Marcu, and B.S.D., manuscript in preparation). To determine the significance of the absence of rT in these tRNAs, we have methylated them enzymatically with a crude preparation of E. coli rT-forming uracil methyltransferase and then compared their efficiency with that of the unmodified tRNAs in a wheat germ cell-free protein synthesising system directed by various natural mRNAs. We report here that these tRNAs function significantly more efficiently in protein synthesis when lacking rT and that the inhibitory effect of rT can be reversed by the polyamine spermine.

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Author notes

  1. KENNETH B. MARCU

    Present address: Institute for Cancer Research, 7701 Burholme Avenue, Fox Chase, Philadelphia, Pennsylvania, 19111

Authors and Affiliations

  1. Biochemistry Department, State University of New York at Stony Brook, Stony Brook, New York, 11794

    KENNETH B. MARCU & BERNARD S. DUDOCK

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  1. KENNETH B. MARCU
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  2. BERNARD S. DUDOCK
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MARCU, K., DUDOCK, B. Effect of ribothymidine in specific eukaryotic tRNAs on their efficiency in in vitro protein synthesis. Nature 261, 159–162 (1976). https://doi.org/10.1038/261159a0

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