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Peptide chain termination. 3. Stimulation of in vitro termination.

Authors
  • Milman, G
  • Goldstein, J
  • Scolnick, E
  • Caskey, T
Type
Published Article
Journal
Proceedings of the National Academy of Sciences of the United States of America
Publication Date
May 01, 1969
Volume
63
Issue
1
Pages
183–190
Identifiers
PMID: 4897024
Source
Medline
License
Unknown

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.

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