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Nucleic Acids Research, 1990, Vol. 18, No. 16 4677-4681
© 1990

Articles

The role of modified purine 64 in initiator/elongator discrimination of tRNAiMet from yeast and wheat germ

Stefan Kiesewetter, Günther Ott and Mathias Sprinzl*

Laboratorium für Biochemie, Universität Bayreuth Universitäts-straße 30, Postfach 10 12 51, D-8580 Bayreuth, FRG

*To whom correspondence should be addressed

Received June 18, 1990. Accepted July 17, 1990.

The role of 2'-ribosylated adenosine 64 in tRNAiMet from yeast in initiation/elongation discrimination was investigated. As measured by in vitro translation in rabbit reticulocyte lysate, the specific removal of the 2'-ribosylphosphate at adenosine 64 via periodate oxidation allows tRNAiMet to read internal AUG codons of the globine messenger RNA. Yeast Met-tRNAiMet lacking the modification of nucleoside 64 forms ternary complexes with GTP and elongation factor Tu from Escherichia coli. The lack of modification at position 64 does not prevent tRNAiMet from participating in the initiation process of in vitro protein synthesis. Wheat germ tRNAiMet has a 2'-ribosylated guanosine at position 64. Removal of this modification from the wheat germ tRNAiMet enables it to read internal AUG codons of globine and tobacco mosaic virus messenger RNA in reticulocyte and wheat germ translation systems, respectively.


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