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Nucleic Acids Research, 1994, Vol. 22, No. 11 1974-1980
© 1994

RNA

Three Tetrahymena tRNAGln isoacceptors as tools for studying unorthodox codon recognition and codon context effects during protein synthesis in vitro

Christine Schüll and Hildburg Beier*

Institut 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 9, 1994. Accepted May 9, 1994.

Three glutamine tRNA isoacceptors are known in Tetrahymena thermophila. One of these has the anticodon UmUG which reads the two normal glutamine codons CAA and CAG, whereas the two others with CUA and UmUA anticodons recognize UAG and UAA, respectively, which serve as termination codons in other organisms. We have employed these tRNAGln-isoacceptors as tools for studying unconventional base interactions in a mRNA- and tRNA-dependent wheat germ extract. We demonstrate here (i) that Formula suppresses the UAA as well as the UAG stop codon, involving a single G:U wobble pair at the third anticodon position and two simultaneous wobble base pairings at the first and third position, respectively, and (ii) that Formula in addition to its cognate codon UAG, reads the UAA stop codon which necessitates a C:A mispairing in the first anticodon position. These unorthodox base interactions take place in a codon context which favours readthrough in tobacco mosaic virus (TMV) or tobacco rattle virus (TRV) RNA, but are not observed in a context that terminates zein and globin protein synthesis. Furthermore, our data reveal that wobble or mispairing in the middle position of anticodon-codon interactions is precluded in either context. The suppressor activities of tRNAsGln are compared with those of other known naturally occurring suppressor tRNAs, i. e., Formula, and Formula. Our results indicate that a ‘leaky’ context is neither restricted to a single stop codon nor to a distinct tRNA species.


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