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Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine

Nature volume 331, pages 723–725 (1988)Cite this article

Abstract

The biological requirement of the trace element selenium was recognized 40 years ago1. Selenium is incorporated into several enzymes and transfer RNA species of both prokaryotic and eukaryotic origin2. In enzymes which contain a selenopolypeptide, selenium is present as covalently bound selenocysteine which participates in the catalytic reaction3. Sequence analysis of the genes coding for two selenoproteins, formate dehydrogenase H from Escherichia coli4 and glutathione peroxidase from mouse5 and man6, demonstrated that an inframe UGA opal nonsense codon directs the incorporation of selenocysteine. In the case of formate dehydrogenase incorporation occurs cotranslationally7. Recently, we identified four genes whose products are required for selenocysteine incorporation in E. coli8 . We report here that one of these genes codes for a tRNA species with unique properties. It possesses an anticodon complementary to UGA and deviates in several positions from sequences, until now, considered invariant in all tRNA species9'10. This tRNA is aminoacylated with L-serine by the seryl-tRNA ligase which also charges cognate tRNASer. Selenocysteine, therefore, is synthesized from a serine residue bound to a natural suppressor tRNA which recognizes UGA.

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Authors and Affiliations

  1. Institut für Genetik und Mikrobiologie der Universität München, Maria-Ward-Strasse la, D-8000, München, 19, FRG

    Walfred Leinfelder, Eva Zehelein & August Bock

  2. Laboratoire de Microbiologie, INSA, 20 Avenue Albert Einstein, F-69621, Villeurbanne Cedex, France

    MarieAndree MandrandBerthelot

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  1. Walfred Leinfelder
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  2. Eva Zehelein
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  3. MarieAndree MandrandBerthelot
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  4. August Bock
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Leinfelder, W., Zehelein, E., MandrandBerthelot, M. et al. Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine. Nature 331, 723–725 (1988). https://doi.org/10.1038/331723a0

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