Title:
Identification of genes influencing synthetic lethality of genetic and epigenetic alterations in translation termination factors in yeast

dc.contributor.author Kiktev, D. A. en_US
dc.contributor.author Chernoff, Yury O. en_US
dc.contributor.author Archipenko, A. V. en_US
dc.contributor.author Zhouravleva, G. A. en_US
dc.contributor.corporatename Sankt-Peterburgskiĭ gosudarstvennyĭ universitet en_US
dc.contributor.corporatename Georgia Institute of Technology. School of Biology en_US
dc.contributor.corporatename Georgia Institute of Technology. Institute for Bioengineering and Bioscience en_US
dc.date.accessioned 2013-08-22T20:16:02Z
dc.date.available 2013-08-22T20:16:02Z
dc.date.issued 2011
dc.description © D.A. Kiktev, Y.O. Chernoff, A.V. Archipenko, G.A. Zhouravleva, 2011 en_US
dc.description DOI: 10.1134/S1607672911030021 en_US
dc.description.abstract Translation termination in eukaryotic cells is determined by proteins Sup35 (eRF3) and Sup45 (eRF1) [1], which interact with a large number of partners [2]. In yeast Saccharomyces cerevisiae, protein Sup35 can form an aggregating epigenetically inherited conformer (prion) [PSI+] [3]. This prion is carried through the cytoplasm and causes disturbances in translation termination, which are phenotypically identified as the dominant omnipotent nonsense suppression. [PSI+] variants with different properties (nonsense suppression efficiency and transmission stability in mitosis) can be obtained in the same yeast strain. The presence of prion [PSI+] leads to lethality in the haploid yeast strain carrying mutations in the gene encoding another termination factor, Sup45 [4]. We have shown that the combination in the diploid strain of some mutant alleles of the SUP45 gene in the heterozygous state with prion [PSI+] entails the death of the hybrid [5]. The synthetic lethality of prion [PSI+] and mutant allele of the sup45 gene depends both on the type of mutant allele and the prion variant. Variant [PSI+], which is a strong suppressor (“strong” [PSI+], or [PSI+]S), causes synthetic lethality with all nonsense mutations and some missense mutations sup45 in the heterozygote. Our data indicate that the lethality of hybrids is correlated with a decreased activity of the Sup45 protein in the cell in case of sup45 mutations. This paper describes a test system that allows identification of proteins that affect the stability of prion [PSI+] and/or the efficiency of translation termination by their effect on the synthetic lethality of the prion conformer Sup35 and mutant alleles of SUP45. This test system is suitable to search for proteins that affect the translation termination efficiency and/ or prion maintenance in yeast cells. Gene library screening using this test system allowed us to identify the CUR1 gene, whose influence on another prion, [URE3], was shown earlier but the effect on translation termination factors was not known. en_US
dc.identifier.citation D.A. Kiktev, Y.O. Chernoff, A.V. Archipenko, G.A. Zhouravleva, "Identification of Genes Influencing Synthetic Lethality of Genetic and Epigenetic Alterations in Translation Termination Factors in Yeast," Dokl Biochem Biophys. Author manuscript; available in PMC 2012 April 9. Published in final edited form as: Dokl Biochem Biophys. 2011 May-Jun; 438: 117–119. Published online 2011 July 3. doi: 10.1134/S1607672911030021 en_US
dc.identifier.doi 10.1134/S1607672911030021
dc.identifier.issn 1607-6729
dc.identifier.uri http://hdl.handle.net/1853/48721
dc.language.iso en_US en_US
dc.publisher Georgia Institute of Technology en_US
dc.publisher.original Russian Academy of Sciences Presidium en_US
dc.subject Yeast en_US
dc.subject Translation termination en_US
dc.subject Eukaryotic cells en_US
dc.subject Protein sequencing en_US
dc.subject Prions en_US
dc.title Identification of genes influencing synthetic lethality of genetic and epigenetic alterations in translation termination factors in yeast en_US
dc.type Text
dc.type.genre Article
dc.type.genre Post-print
dspace.entity.type Publication
local.contributor.author Chernoff, Yury O.
local.contributor.corporatename College of Sciences
local.contributor.corporatename School of Biological Sciences
relation.isAuthorOfPublication d9f3d192-f4c7-4db2-ace4-2baadbeb98b6
relation.isOrgUnitOfPublication 85042be6-2d68-4e07-b384-e1f908fae48a
relation.isOrgUnitOfPublication c8b3bd08-9989-40d3-afe3-e0ad8d5c72b5
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