The influence of 5 ' codon context on translation termination in Saccharomyces cerevisiae

Mottagui-Tabar, Salim and Tuite, Mick F. and Isaksson, Lief 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. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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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: 02 May 2014 14:20
Resource URI: https://kar.kent.ac.uk/id/eprint/17460 (The current URI for this page, for reference purposes)
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