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Nucleic Acids Research, 1990, Vol. 18, No. 3 487-491
© 1990

MOLECULAR BIOLOGY

Interaction of a selenocysteine-incorporating tRNA with elongation factor Tu from E.coli

Charlotte Förster, Günther ott, Karl Forchhammer1 and Mathias Sprinzl*

Laboratorium für Biochemie der Universität Bayreuth Postfach 10 12 51, D-8580 Bayreuth 1Lehrstuhl für Mikrobiologie der Universität München Maria-Ward-Strasse la, D-8000 Munich 19, FRG

* To whom correspondence should be addressed

Received October 30, 1989. Accepted January 3, 1990.

Selenocysteine-incorporating tRNASec(UCA), the product of selC, was isolated from E.coli and aminoacylated with serine. The equilibrium dissociation constant for the interaction of Ser- tRNASec(UCA) with elongation factor Tu GTP was determined to be 5.0±2.5x10–8 M. Compared with the dissociation constants of the two elongator Ser-tRNASer species (Kd = 7 x 10–10 M), the selenocysteine-incorporating UGA suppressor tRNA has an almost hundred fold weaker affinity for EF-Tu·GTP. This suggests a mechanism by which the Ser-tRNASec is prevented in recognition of UGA codons. This tRNA is not bound to EF-Tu·GTP and is converted to selenocysteinyl-tRNASec. We also demonstrate the lack of an efficient interaction of Sec with EF-Tu·GTP. The results of this work are in support of a mechanism by which the selenocysteine incorporation at UGA nonsense codons is mediated by an elongation factor other than EF-Tu·GTP.


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