Abstract

Bacteriophage T4 α-glucosyl transferase mRNA is made as a polycistronic 21S molecule that is processed during normal infection to the commonly found 14.5S species. By using antibiotic inhibitors of protein synthesis, it is possible to distinguish two steps involved in the processing of the 21S polycistronic α-gt mRNA in T4-infected Escherichia coli . There is an initial cleavage to an 18S molecule that does not require protein synthesis. However, the next step, the conversion of the 18S into the 14.5S molecule, requires simultaneous protein synthesis.

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