Mottagui-Tabar, S. and Tuite, M.F. and Isaksson, L.A. (1998) The influence of 5 ' codon context on translation termination in Saccharomyces cerevisiae. European Journal of Biochemistry, 257 (1). pp. 249-254. ISSN 0014-2956.
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| Official URL http://dx.doi.org/10.1046/j.1432-1327.1998.2570249... |
Abstract
Translation termination in vivo was studied in the yeast Saccharomyces cerevisiae using a translation-assay system. Codon changes that were made at position -2-relative to the stop codon, gave a 3.5-fold effect on termination in a release-factor-defective (sup45) mutant strain, in line with the effect observed in a wild-type strain. The influence of the -2 codon could be correlated to the charge of the corresponding amino acid residue in the nascent peptide; an acidic residue favoring efficient termination. Thus, the C-terminal end of the nascent peptide influences translation termination both in the bacterium Escherichia coil and to a lesser extent in the yeast S. cerevisiae. However, the sensitivity to the charge of the penultimate amino acid is reversed when the E. coli and S. cerevisiae are compared. Changing -1 (P-site) codons in yeast gave a 10-fold difference in effect on the efficiency of termination. This effect could not be related to any property of the encoded last amino acid in the nascent peptide. Iso-codons read by the same tRNA (AAA/G, GAA/G) gave similar readthrough values. Codons for glutamine (CAA/G), glutamic acid (GAA/G) and isoleucine (AUA/C) that are read by different isoaccepting tRNAs are associated with an approximately twofold difference in each case in termination efficiency. This suggests that the P-site tRNAis able to influence termination at UGAC in yeast.
| Item Type: | Article |
|---|---|
| Uncontrolled keywords: | 5 ' codon context; tRNA; translation termination; nascent peptide; release factor; yeast |
| Subjects: | Q Science |
| Divisions: | Faculties > Science Technology and Medical Studies > School of Biosciences |
| Depositing User: | M.A. Ziai |
| Date Deposited: | 06 Oct 2009 08:19 |
| Last Modified: | 06 Oct 2009 08:19 |
| Resource URI: | http://kar.kent.ac.uk/id/eprint/17460 (The current URI for this page, for reference purposes) |
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