Abstract
A formylmethionyl-tRNA f deacylase has been purified about 330-fold from a crude initiation factor preparation (1 M NH 4Cl ribosomal wash) from Escherichia coli Q13. The enzyme was nearly homogeneous and had an apparent molecular weight of 24 000. Rat liver methionyl-tRNA f and E. coli methionyl-tRNA m were not hydrolyzed significantly by the enzyme under standard conditions. Qβ RNA- and AUG(A) n-directed polypeptide synthesis was inhibited by the enzyme. The inhibition was at the level of initiation of polypeptide synthesis. The enzymatic activity was inhibited by various factors necessary for polypeptide synthesis. The activity was inhibited more by NH 4Cl and spermidine than by Mg 2+, GTP and ATP. The complex of formylmethionyl-tRNA f, initiation factor 2 and GTP was resistant to enzymatic hydrolysis, and the resistance was enhanced by the addition of AUG and ribosomes to the above reaction mixture.
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