Accumulation of tRNAMetf on 80-S ribosomes in vitro under the influence of a Met-tRNA deacylase from rat-liver microsomes.

A Met-tRNA deacylase has been partially purified from the 0.5 M KCl wash of rat liver microsomes. In preparative sucrose gradients, the active component sediments as a single band at about 6 S, corresponding to an estimated molecular weight of 1.7 X 10(5). The deacylase is specific for Met-tRNA, without discriminating between Met-tRNA f and Met-tRNAm. Met-tRNAf bound to the initiation factor IF-MP in the ternary complex, IF-MP-GTP-Met-tRNAf, or to initiation-factor-dependent, complexes with 40-S subunits or 80-S ribosomes, is protected against deacylation. However, in the course of the initiation-factor-dependent joining of the 40-S subunit complex to 60-S ribosomal subunits, the bound Met-tRNAf is exposed to added deacylase. Under these conditions, deacylation is inhibited by GTP. The tRNAMetf remains bound and accumulates on the 80-S ribosomes.