Abstract
Translation termination requires two codon-specific polypeptide release factors in prokaryotes and one omnipotent factor in eukaryotes. Sequences of 17 different polypeptide release factors from prokaryotes and eukaryotes were compared. The prokaryotic release factors share residues split into seven motifs. Conservation of many discrete, perhaps critical, amino acids is observed in eukaryotic release factors, as well as in the C-terminal portion of elongation factor (EF) G. Given that the C-terminal domains of EF-G interacts with ribosomes by mimicry of a tRNA structure, the pattern of conservation of residues in release factors may reflect requirements for a tRNA-mimicry for binding to the A site of the ribosome. This mimicry would explain why release factors recognize stop codons and suggests that all prokaryotic and eukaryotic release factors evolved from the progenitor of EF-G.
Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 10:34 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 2 p.m.) |
Indexed | 1 month, 2 weeks ago (July 11, 2025, 6:35 a.m.) |
Issued | 29 years, 3 months ago (May 28, 1996) |
Published | 29 years, 3 months ago (May 28, 1996) |
Published Online | 29 years, 3 months ago (May 28, 1996) |
Published Print | 29 years, 3 months ago (May 28, 1996) |
@article{Ito_1996, title={Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis.}, volume={93}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.93.11.5443}, DOI={10.1073/pnas.93.11.5443}, number={11}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Ito, K and Ebihara, K and Uno, M and Nakamura, Y}, year={1996}, month=may, pages={5443–5448} }