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Nucleic Acids Research, 1993, Vol. 21, No. 24 5679-5683
© 1993

RNA

Discrimination between initiation and elongation of protein biosynthesis in yeast: identity assured by a nucleotide modification in the initiator tRNA

C. Foürster, K. Chakraburtty1 and M. Sprinzl*

Laboratorium fuür Biochemie, Universitaüt Bayreuth 95440 Bayreuth, Germany 1Department of Biochemistry, Medical College of Wisconsin Milwaukee, Wl 53226, USA

*To whom correspondence should be addressed

Received August 24, 1993. Revised November 2, 1993. Accepted November 2, 1993.

Cytoplasmic initiator tRNAs from plants and fungi possess an unique 2'-phosphoribosyl residue at position 64 of their sequence. In yeast tRNAiMet, this modified nucleoside located in the T-stem of the tRNA is a 2'-1 ''-(ß-O-ribofuranosyl-5''-phosphoryl)-adenosine. The phosphoribosyl residue of this modified nucleoside was removed chemically by treatment involving periodate oxidation of tRNAiMet and regeneration of the 3'-terminal adenosine with ATP(CTP):tRNA nucleotidyl transferase. The role of phosphoribosylation at position 64 for interaction with elongation factor eEF-1{alpha} and initiation factor 2 (elF-2) was investigated in the homologous yeast system. Whereas the 5'-phosphoribosyl residue prevents the binding of MettRNAiMet to eEF-1{alpha}, it does not influence the interaction with elF-2. After removal of the ribosyl group, the demodified initiator tRNA showed binding to eEF-1{alpha}, but no change was detected with respect to the interaction with the initiation factor elF-2. This observation is interpreted to mean that a single modification of an eucaryotic initiator tRNA in yeast serves as a negative discriminant for eEF-1{alpha}, thus preventing the initiator tRNAiMet from entering the elongation cycle of protein biosynthesis.


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