PEPTIDE CHAIN TERMINATION, V. THE ROLE OF RELEASE FACTORS IN MRNA TERMINATOR CODON RECOGNITION
- 1 December 1969
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 64 (4) , 1235-1241
- https://doi.org/10.1073/pnas.64.4.1235
Abstract
The protein release factors, R1 and R2, bind to ribosomes in response to specific terminator codons (R1 to UAA or UAG, R2 to UAA or UGA). In reactions containing ribosomes, the tritiated oligonucleotide UA[(3)H](A)(2) is retained on nitrocellulose filters in response to either R1 or R2, and UA[(3)H]G in response to R1. These results indicate that an R.terminator codon.70S ribosome intermediate occurs during terminator codon recognition and suggest that protein release factors R1 and R2 recognize terminator codons.Keywords
This publication has 12 references indexed in Scilit:
- Recognition of Nucleotide SequencesAnnual Review of Biochemistry, 1969
- Sequential Translation of Trinucleotide Codons for the Initiation and Termination of Protein SynthesisScience, 1968
- Release factors differing in specificity for terminator codons.Proceedings of the National Academy of Sciences, 1968
- Requirement of granosine 5'-triphosphate for ribosomal binding of aminoacyl-SRNA.Proceedings of the National Academy of Sciences, 1968
- Polypeptide chain termination in vitro: isolation of a release factor.Proceedings of the National Academy of Sciences, 1967
- Ribosome-catalysed peptidyl transfer: Effects of some inhibitors of protein synthesisJournal of Molecular Biology, 1967
- Regulatory mechanisms and protein synthesis X. Codon recognition on 30 s ribosomesJournal of Molecular Biology, 1966
- The RNA Code and Protein SynthesisCold Spring Harbor Symposia on Quantitative Biology, 1966
- Oligonucleotide-Ribosome-AA-sRNA InteractionsCold Spring Harbor Symposia on Quantitative Biology, 1966
- Synthesis of Trinucleoside Diphosphates with Polynucleotide Phosphorylase*Biochemistry, 1965