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The dependence of mitochondrial protein synthesis initiation upon the formylation of initiator met-tRNA was investigated in experiments in which the rate of formyl-methionyl-peptidyl-puromycin derivatives formation was measured in the presence or absenceof the appropriate formylating agent. The presence on N-formyl-THFA increases several times the amount of C-Met incorporation in the initial peptides: in addition, when N-C-formyl-THFA was supplied, a remarkable amount of radioactivity was recovered...
The properties of N-formyl-tetrahydrofolate: methionyl-tRNA transformylase from Euglena gracilis were studied and compared with those of the E. coli enzyme. The Euglena enzyme, functioning in formylation of met-tRNA initiator of organellar protein synthesis, shows a partial requirement of Mg, with an optimum of 5 mM, stimulation by K, Km for N-formyl-THFA 2.5 x 10 M. These properties are different from those of the bacterial enzyme. For example the affinity for the substrate N-formyl-THFA is significantly...
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