Modified aminoacyl-tRNA. IV. The behaviour of acyl[14C]phenylalanyl-tRNA in a ribosomal system from wheat germ

N. De Groot*, A. Panet, I. Fry-Shafrir, Y. Lapidot

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The binding of acyl[14C]phenylalanyl-tRNA to wheat germ ribosomes was studied. Acyl[14C]phenylalanyl-tRNA binds less tightly to the ribosomes in the presence of poly U than the parent [14C]phenylalanyl-tRNA. Uncharged tRNA inhibits the binding of acyl[14C]phenylalanyl-tRNA more than the binding of [14C]phenylalanyl-tRNA. GTP, at a low concentration (10 μM), inhibits the binding of acyl[14C]phenylalanyl-tRNA but not that of [14C]phenylalanyl-tRNA. A 14C-labelled peptide is formed from acyl[14C]phenylalanyl-tRNA only if ribosomes, poly U and acyl[14C]phenylalanyl-tRNA are incubated prior to adding all the other components of the incorporation reaction. The peptide formed from acyl[14C]phenylalanyl-tRNA has a blocked terminal amino group and internal phenylalanyl residues are labelled. At 0.004 M magnesium acetate, the amount of [14C]phenylalanine incorporated from acyl[14C]phenylalanyl-tRNA is higher than that from [14C]phenylalanyl-tRNA under identical reaction conditions.

Original languageEnglish
Pages (from-to)137-146
Number of pages10
JournalBBA Section Nucleic Acids And Protein Synthesis
Volume161
Issue number1
DOIs
StatePublished - 18 Jun 1968

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