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J. Biol. Chem., Vol. 259, Issue 8, 4706-4709, 04, 1984

Isoleucyl initiator tRNA does not initiate eucaryotic protein synthesis

T Wagner, M Gross and PB Sigler

Initiator tRNA from yeast (tRNAMeti) was quantitatively misaminoacylated with L-isoleucine using isoleucyl-tRNA synthetase from Escherichia coli. Surprisingly the misaminoacylated Ile-tRNAMeti neither participates in nor inhibits the initiation of globin synthesis in a rabbit reticulocyte lysate, whereas Met-tRNAMeti readily initiates protein synthesis in the same system. The incompetent behavior of Ile- tRNAMeti may be related to the observation that in vitro it does not form a stable complex with eucaryotic initiation factor 2 (eIF-2) and GTP, under conditions which lead to a stable eIF-2 X GTP X Met-tRNAMeti ternary complex. This indicates that eIF-2 can discriminate between the side chains of the aminoacyl adducts of the tRNAMeti during ternary complex formation, the first essential step in initiation of eucaryotic protein synthesis.
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