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Nucleic Acids Research Advance Access originally published online on January 27, 2009
Nucleic Acids Research 2009 37(6):1789-1798; doi:10.1093/nar/gkp012
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Nucleic Acids Research, 2009, Vol. 37, No. 6 1789-1798
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

RNA

Molecular dissection of translation termination mechanism identifies two new critical regions in eRF1

Isabelle Hatin, Celine Fabret, Jean-Pierre Rousset and Olivier Namy*

Univ Paris-Sud and IGM, CNRS, UMR 8621, Orsay, F 91405, France

*To whom correspondence should be addressed. Tel: +33 169 154 634; Fax: +33 169154 629; Email: olivier.namy{at}igmors.u-psud.fr

Received September 23, 2008. Revised January 5, 2009. Accepted January 7, 2009.

Translation termination in eukaryotes is completed by two interacting factors eRF1 and eRF3. In Saccharomyces cerevisiae, these proteins are encoded by the genes SUP45 and SUP35, respectively. The eRF1 protein interacts directly with the stop codon at the ribosomal A-site, whereas eRF3—a GTPase protein—probably acts as a proofreading factor, coupling stop codon recognition to polypeptide chain release. We performed random PCR mutagenesis of SUP45 and screened the library for mutations resulting in increased eRF1 activity. These mutations led to the identification of two new pockets in domain 1 (P1 and P2) involved in the regulation of eRF1 activity. Furthermore, we identified novel mutations located in domains 2 and 3, which confer stop codon specificity to eRF1. Our findings are consistent with the model of a closed-active conformation of eRF1 and shed light on two new functional regions of the protein.


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