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. 1969 May;63(1):183–190. doi: 10.1073/pnas.63.1.183

PEPTIDE CHAIN TERMINATION, III. STIMULATION OF in vitro TERMINATION

G Milman 1,*, J Goldstein 1, E Scolnick 1, T Caskey 1
PMCID: PMC534020  PMID: 4897024

Abstract

Throughout extensive purification, the release factors R1 and R2 each behave as a single molecular species with alternate codon recognition (R1, UAA or UAG; R2, UAA or UGA). The release of f[3H]methionine from f[3H]-Met-tRNA·AUG·ribosome complex requires R factor and terminator codon and does not appear to require tRNA or transfer factors T and G. Purification of the components of the release assay has enabled identification of a protein factor S in the 55-80 per cent ammonium sulfate fraction of E. coli B supernatant fraction which stimulates the rate but not the extent of release dependent upon R factor and appropriate termination codon. The S factor has properties similar to T, but further purification is required to determine the nature and function of S in peptide chain termination.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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