Abstract
Three species of tRNA capable of being aminoacylated with methionine have been isolated from a crude tRNA fraction of the brewers yeast ( Saccharomyces cerevisiae) after chromatography on benzolyated DEAE-cellulose. These three species of tRNA Met can be distinguished on the basis of several criteria. They differ in their ability to be aminoacylated with Escherichia coli aminoacyl-tRNA synthetase; to be formylated by E. coli transformylase; to participate in in vitro protein synthesis in a yeast system based on endogenous mRNA; and to take part in a GTP factor-dependent binding reaction to yeast ribosomes. They also differ in their abilities to bind to 80 S ribosomes or 40 S ribosomal subunits in a reaction that does not contain GTP and is carried out at high Mg 2+. The methionine-containing oligonucleotides isolated after the ribonuclease T 1 digestion of each methionyl-tRNA have different electrophoretic mobilities. Fraction 1 of these species acts in a manner similar to initiator tRNAs of other eucaryotic and procaryotic systems when tested in a homologous yeast system. Fractions 2 and 3 appear to represent the species of tRNA Met that are concerned with the translation of the internal methionine codons.
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