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Biosynthesis of Phage-specific Initiation Dipeptides

A PURIFIED BIOSYNTHETIC SYSTEM DERIVED FROM ESCHERICHIA COLI

From the ¹ From the Section on Molecular Genetics, Laboratory of Biomedical Sciences, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20014

This report describes the properties of a purified Escherichia coli protein synthetic system which accurately translates the initial codons of the bacteriophage f₂ maturation, coat, and RNA synthetase cistrons. In order to assay cistron recognition easily and to accumulate specific intermediates in the translation of a natural message, we have restricted in vitro synthesis to the formation of the initial formyldipeptides corresponding to the three f₂ cistrons. This is accomplished by preventing the initial, G factor-requiring translocation reaction through the use of small amounts of monospecific anti-G factor antibody or the antibiotic fusidic acid. The reaction requires initiation-competent ribosomes which are depleted of elongation factors by repeated washings in low ionic strength buffer. Initiation in this system is quite specific. The initial f₂ coat dipeptide, N-formylmethionylalanine, is readily converted into the expected coat tripeptide, N-formylmethionylalanylserine, if translocation is permitted. In addition, synthesis of the initial f₂ RNA synthetase dipeptide, N-formylmethionylserine, is specifically repressed in the presence of f₂ coat protein, indicating that this purified system is sensitive to translational control.

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