PEPTIDE CHAIN TERMINATION, III. STIMULATION OF in vitro TERMINATION
AUTOR(ES)
Milman, G.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=534020Documentos Relacionados
- Peptide Chain Termination, VI. Purification and Site of Action of S
- Peptide Chain Termination, VII. The Ribosomal and Release Factor Requirements for Peptide Release
- PEPTIDE CHAIN TERMINATION, V. THE ROLE OF RELEASE FACTORS IN MRNA TERMINATOR CODON RECOGNITION
- Mammalian Peptide Chain Termination, II. Codon Specificity and GTPase Activity of Release Factor
- Specific termination of in vitro transcription by calf thymus RNA polymerase III.