Publication: The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae
Issued Date
1999-05-29
Resource Type
ISSN
0950382X
Other identifier(s)
2-s2.0-0032937983
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Molecular Microbiology. Vol.32, No.3 (1999), 485-496
Suggested Citation
Lily Eurwilaichitr, Fiona M. Graves, Ian Stansfield, Mick F. Tuite The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae. Molecular Microbiology. Vol.32, No.3 (1999), 485-496. doi:10.1046/j.1365-2958.1999.01346.x Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/25338
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae
Other Contributor(s)
Abstract
Translation termination in eukaryotes is mediated by two release factors, eRF1 and eRF3, which interact to form a heterodimer that mediates termination at all three stop codons. By C-terminal deletion analysis of eRF1 from the yeast Saccharomyces cerevisiae, we show that the extreme C-terminus of this 437-amino-acid protein defines a functionally important domain for translation termination. A strain encoding eRF1 lacking the C-terminal 32 amino acids is not viable, whereas deletion of the C-terminal 19 amino acids is viable but shows a termination defect in vivo causing an enhancement of nonsense suppression. Using a combination of two-hybrid analysis and in vitro binding studies, we demonstrate that deletions encompassing the C-terminus of eRF1 cause a significant reduction in eRF3 binding to eRF1. All of the C-terminally truncated eRF1 still bind the ribosome, suggesting that the C-terminus does not constitute a ribosome-binding domain and eRF1 does not need to form a stable complex with eRF3 in order to bind the ribosome. These data, together with previously published data, suggest that the region between amino acids 411 and 418 of yeast eRF1 defines an essential functional domain that is part of the major site of interaction with eRF3. However, a stable eRF1:eRF3 complex does not have to be formed to maintain viability or efficient translation termination. Alignment of the seven known eukaryotic eRF1 sequences indicates that a highly conserved motif, GFGGIGG/A is present within the region of the C-terminus, although our deletion studies suggest that it is sequences C-terminal to this region that are functionally important.