PEPTIDE CHAIN TERMINATION, III. STIMULATION OF in vitro TERMINATION
- 1 May 1969
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 63 (1), 183-190
- https://doi.org/10.1073/pnas.63.1.183
Abstract
Throughout extensive purification, the release factors R(1) and R(2) each behave as a single molecular species with alternate codon recognition (R(1), UAA or UAG; R(2), UAA or UGA). The release of f[(3)H]methionine from f[(3)H]-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.Keywords
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