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Nucleic Acids Research, 1994, Vol. 22, No. 12 2228-2233
© 1994

RNA

Eukaryotic selenocysteine inserting tRNA species support selenoprotein synthesis in Escherichia coli

Christian Baron+,, Christine Sturchler1, Xin-Qi Wu2,§, Hans J. Gross2, Alain Krol1 and August Böck*,

Lehrstuhl für Mikrobiologie der Universität München Maria-Ward-Straße 1a, D-80638 München, Germany 1UPR ‘Structure des Macromolécules Biologiques et Mécanismes de Reconnaissance’, Institut de Biologie Moléculaire et Cellulaire du CNRS 15 rue René Descartes, F-67084 Strasbourg Cedex, France 2Institut für Biochemie, Bayerische Julius-Maximilians-Universität, Biozentrum Am Hubland, D-97074 Würzburg, Germany

*To whom correspondence should be addressed

Received April 8, 1994. Revised May 20, 1994. Accepted May 20, 1994.

Although the tRNA species directing selenocysteine insertion in prokaryotes differ greatly in their primary structure from that of their eukaryotic homologues they share very similar three-dimensional structures. To analyse whether this conservation of the overall shape of the molecules reflects a conservation of their functional interactions it was tested whether the selenocysteine inserting tRNA species from Homo sapiens supports selenoprotein synthesis in E.coli. It was found that the expression of the human tRNASec gene in E.coli can complement a lesion in the tRNASec gene of this organism. Transcripts of the Homo sapiens and Xenopus laevis tRNASec genes synthesised in vitro were amino-acylated by the E.coli seryl-tRNA ligase although at a very low rate and the resulting seryl-tRNASec was bound to and converted into selenocysteyl-tRNASec by the selenocysteine synthase of this organism. Selenocysteyl-tRNASec from both eukaryotes was able to form a complex with translation factor SELB from E.coli. Although the mechanism of selenocysteine incorporation into seleno-proteins appears to be rather different in E.coli and in vertebrates, we observe here a surprising conservation of functions over an anourmous evolutionary distance.

+Present addresses: Department of Plant Biology, 111 Koshland Hall, University of California, Berkeley, CA 94720

§Department of Biology, Massachusetts Institute of Biology, Cambridge, MA 02139, USA


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