How does Euplotes translation termination factor eRF1 fail to recognize the UGA stop codon?

التفاصيل البيبلوغرافية
العنوان: How does Euplotes translation termination factor eRF1 fail to recognize the UGA stop codon?
المؤلفون: L. Bidou, Peter M. Kolosov, L. Yu. Frolova, Jean-Pierre Rousset, Lev L. Kisselev, Sergey Lekomtsev
المصدر: Molecular Biology. 41:924-931
بيانات النشر: Pleiades Publishing Ltd, 2007.
سنة النشر: 2007
مصطلحات موضوعية: chemistry.chemical_classification, Genetics, Biophysics, Biology, Genetic code, biology.organism_classification, Fusion protein, Stop codon, Amino acid, Open reading frame, chemistry, Structural Biology, Stylonychia, Release factor, Sequence (medicine)
الوصف: Class 1 eukaryotic release factor 1 (eRF1) recognizes all three stop codons (UAA, UAG, and UGA) in standard-code organisms. In some ciliates with variant genetic codes, one or two stop codons are used to encode amino acids and are not recognized by eRF1; e.g., UAA and UAG are reassigned to Gln in Stylonychia and UGA is reassigned to Cys in Euplotes. Stop codon recognition is due to the N-terminal domain of eRF1 in standard-code organisms. Since variant-code ciliates most likely originate from universal-code ancestors, the N-domain sequence of their eRF1 was assumed to harbor the residues that are responsible for the changes in stop codon recognition specificity. To identify the N-domain regions determining the UGA-only specificity of Euplotes aediculatus eRF1, chimeric proteins were constructed by swapping various N-domain fragments of the E. aediculatus for their human counterparts; the MC domain was from human eRF1. Functional analysis of the chimeric eRF1 in vivo revealed two regions (residues 38–50 and 123–145) restricting the E. aediculatus eRF1 specificity to UAR. The change in stop codon recognition specificity of eRF1 was regarded as the first step in the origin of the variant genetic code in ciliates.
تدمد: 1608-3245
0026-8933
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::83bc5b6fa4f5572c9d5e53d24b9cdde9
https://doi.org/10.1134/s002689330706009x
حقوق: CLOSED
رقم الأكسشن: edsair.doi...........83bc5b6fa4f5572c9d5e53d24b9cdde9
قاعدة البيانات: OpenAIRE