Abstract
Peptide synthesis in eukaryotes terminates when eukaryotic release factor 1 (eRF1) binds to an mRNA stop codon and occupies the ribosomal A site. Domain 1 of the eRF1 protein has been implicated in stop codon recognition in a number of experimental studies. In order to further pinpoint the residues of this protein involved in stop codon recognition, we sequenced and compared eRF1 genes from a variety of ciliated protozoan species. We then performed a series of computational analyses to evaluate the conservation, accessibility, and structural environment of each amino acid located in domain 1. With this new dataset and methodology, we were able to identify eight specific amino acid sites important for stop codon recognition and also to propose a set of cooperative paired substitutions that may underlie stop codon reassignment. Our results are more consistent with current experimental data than previously described models.
Original language | English (US) |
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Pages (from-to) | 337-344 |
Number of pages | 8 |
Journal | Journal of Molecular Evolution |
Volume | 60 |
Issue number | 3 |
DOIs | |
State | Published - Mar 2005 |
Externally published | Yes |
Keywords
- Ciliates
- Eukaryotic release factor 1
- Genetic code
- Hypotrich
- Spirotrich
- Stichotrich
- Stop codon reassignment
- Translation termination
ASJC Scopus subject areas
- Ecology, Evolution, Behavior and Systematics
- Molecular Biology
- Genetics