Boreskov

OP‐30ConclusionSuccessive duplications of genes encoding elongation factors for translation led to theemergence of several protein complexes with different properties. The eRF1‐eRF3 complexterminates translation, and the Dom34‐Hbs1 complex is involved in the quality control ofmRNA. Both eRF1 and eRF3 interact not only with each other but also with additionalproteins. Some of these interactions are possibly mutually exclusive, and some of theproteins interacting with eRF1/eRF3 can be components of the complex terminatingtranslation.AcknowledgmentsThis work was supported by the Russian Foundation for Basic Research (10‐04‐00237)and the Program of the Presidium of the Russian Academy of Sciences, The Origin and theEvolution of the Biosphere.References[1]. Inagaki Y, Doolittle WF: Evolution of the eukaryotic translation termination system: origins of releasefactors. Mol Biol Evol 2000, 17: 882‐889.[2]. Nakamura Y, Ito K: How protein reads the stop codon and terminates translation. Genes Cells 1998, 3: 265‐278.[3]. Saito K, Kobayashi K, Wada M, Kikuno I, Takusagawa A, Mochizuki M et al.: Omnipotent role of archaealelongation factor 1 alpha (EF1alpha in translational elongation and termination, and quality control ofprotein synthesis. Proc Natl Acad Sci U S A 2010, 107: 19242‐19247.[4]. Atkinson GC, Baldauf SL, Hauryliuk V: Evolution of nonstop, no‐go and nonsense‐mediated mRNA decayand their termination factor‐derived components. BMC Evol Biol 2008, 8: 290.[5]. Liang A, Brunen‐Nieweler C, Muramatsu T, Kuchino Y, Beier H, Heckmann K: The ciliate Euplotesoctocarinatus expresses two polypeptide release factors of the type eRF1. Gene 2001, 262: 161‐168.[6]. Chapman B, Brown C: Translation termination in Arabidopsis thaliana: characterisation of three versions ofrelease factor 1. Gene 2004, 341: 219‐225.[7]. Chauvin C, Salhi S, Le Goff C, Viranaicken W, Diop D, Jean‐Jean O: Involvement of human release factorseRF3a and eRF3b in translation termination and regulation of the termination complex formation. Mol CellBiol 2005, 25: 5801‐5811.[8]. Hoshino S, Imai M, Mizutani M, Kikuchi Y, Hanaoka F, Ui M et al.: Molecular cloning of a novel member ofthe eukaryotic polypeptide chain‐releasing factors (eRF). Its identification as eRF3 interacting with eRF1. JBiol Chem 1998, 273: 22254‐22259.[9]. Czaplinski K, Ruiz‐Echevarria MJ, Paushkin SV, Han X, Weng Y, Perlick HA et al.: The surveillance complexinteracts with the translation release factors to enhance termination and degrade aberrant mRNAs. GenesDev 1998, 12: 1665‐1677.[10]. Wang W, Czaplinski K, Rao Y, Peltz SW: The role of Upf proteins in modulating the translation read‐throughof nonsense‐containing transcripts. EMBO J 2001, 20: 880‐890.[11]. Doma MK, Parker R: Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation.Nature 2006, 440: 561‐564.[12]. Vasudevan S, Peltz SW, Wilusz CJ: Non‐stop decay‐‐a new mRNA surveillance pathway. Bioessays 2002, 24:785‐788.[13]. van Hoof A, Frischmeyer PA, Dietz HC, Parker R: Exosome‐mediated recognition and degradation ofmRNAs lacking a termination codon. Science 2002, 295: 2262‐2264.82