IDENTIFICATION OF PEPTIDES SYNTHESIZED BY THE CELL-FREE E. COLI SYSTEM WITH POLYNUCLEOTIDE MESSENGERS

Abstract
Tryptlc hydrolysis of the tungstic-acid-insoluble product of lysine incorporation by the cell-free Escherichia coli system (in the presence of poly-A) yielded dilysine and trilyslne thus characterizing the product as poly-L-lysine. Tryptic hydrolysis of the tungstic-acid-insoluble products synthesized, in the presence of poly AU (51), from a mixture of asparagine, isoleuclne, leucine, lysine, phenylalanine and tyrosine (some of which were labeled with C14) yielded a series of radioactive peptides which (upon acid hydrolysis) released radioactive lysine and isoleuclne, or lysine and asparagine. This shows that poly AU (a copolynucleotide of adenylic-and uridylic-acid) directs the synthesis of lysine-containing copolypeptides by the E. coli system.

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