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

Authors
Type
Published Article
Journal
Proceedings of the National Academy of Sciences of the United States of America
Publication Date
Volume
63
Issue
1
Pages
183–190
Identifiers
PMID: 4897024
Source
Medline

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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