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Ribosome-catalyzed formation of an abnormal peptide analogue

Journal Article · · Biochemistry; (United States)
OSTI ID:6525149
The peptidyl-tRNA analogue N-(chloracetyl) phenylalanyl-tRNA/sup Phe/ was prepared by chemical aminoacylation and prebound to the P site of Escherichia coli ribosomes in response to poly(uridylic acid). Admixture of phenylalanyl-tRNA/sup Phe/ to the A site resulted in the formation of two dipeptides, one of which was found by displacement of chloride ion from the peptidyl-tRNA. This constitutes the first example of ribosome-mediated formation of a peptide of altered connectivity and suggests a need for revision of the current model of peptide bond formation. Also suggested by the present finding is the feasibility of utilizing tRNAs to prepare polypeptides of altered connectivity in an in vitro protein biosynthesizing system. (/sup 32/P)-oligo(rA), (/sup 3/H)- and (/sup 14/C) phenylalanines were used in the assay of the peptidye-tRNA analogue.
Research Organization:
Univ. of Virginia, Charlottesville
OSTI ID:
6525149
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 25:21; ISSN BICHA
Country of Publication:
United States
Language:
English