Abstract
Peptide chain termination is a result of at least two events: terminator codon recognition and hydrolysis of peptidyl tRNA. A protein factor S , isolated from the supernatant of Escherichia coli B, stimulates fMet release. Factor S lowers the K m for terminator trinucleotides without altering the V max of release and therefore acts at terminator codon recognition. The S protein differs from initiation factors, elongation factor G , several forms of elongation factor T and release factors. The importance of the 2% Tu content in purified S is unresolved.
Dates
Type | When |
---|---|
Created | 19 years, 3 months ago (May 31, 2006, 2:18 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 10:39 a.m.) |
Indexed | 1 month, 4 weeks ago (July 2, 2025, 2:46 p.m.) |
Issued | 55 years, 7 months ago (Feb. 1, 1970) |
Published | 55 years, 7 months ago (Feb. 1, 1970) |
Published Online | 55 years, 7 months ago (Feb. 1, 1970) |
Published Print | 55 years, 7 months ago (Feb. 1, 1970) |
@article{Goldstein_1970, title={Peptide Chain Termination, VI. Purification and Site of Action of S}, volume={65}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.65.2.430}, DOI={10.1073/pnas.65.2.430}, number={2}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Goldstein, J. and Milman, G. and Scolnick, E. and Caskey, T.}, year={1970}, month=feb, pages={430–437} }