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Positioning of CCA-arms of the A- and the P-tRNAs towards the 28S rRNA in the human ribosome.
Bulygin, Konstantin; Malygin, Alexey; Hountondji, Codjo; Graifer, Dmitri; Karpova, Galina.
Afiliación
  • Bulygin K; Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, pr. Lavrentieva, 8, 630090 Novosibirsk, Russia.
Biochimie ; 95(2): 195-203, 2013 Feb.
Article en En | MEDLINE | ID: mdl-23023194
Nucleotides of 28S rRNA involved in binding of the human 80S ribosome with acceptor ends of the A site and the P site tRNAs were determined using two complementary approaches, namely, cross-linking with application of tRNA(Asp) analogues substituted with 4-thiouridine in position 75 or 76 and hydroxyl radical footprinting with the use of the full sized tRNA and the tRNA deprived of the 3'-terminal trinucleotide CCA. In general, these 28S rRNA nucleotides are located in ribosomal regions homologous to the A, P and E sites of the prokaryotic 50S subunit. However, none of the approaches used discovered interactions of the apex of the large rRNA helix 80 with the acceptor end of the P site tRNA typical with prokaryotic ribosomes. Application of the results obtained to available atomic models of 50S and 60S subunits led us to a conclusion that the A site tRNA is actually present in both A/A and A/P states and the P site tRNA in the P/P and P/E states. Thus, the present study gives a biochemical confirmation of the data on the structure and dynamics of the mammalian ribosomal pretranslocation complex obtained with application of cryo-electron microscopy and single-molecule FRET [Budkevich et al., 2011]. Moreover, in our study, particular sets of 28S rRNA nucleotides involved in oscillations of tRNAs CCA-termini between their alternative locations in the mammalian 80S ribosome are revealed.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ribosomas / Tiouridina / Biosíntesis de Proteínas / ARN de Transferencia de Aspártico Límite: Animals / Humans Idioma: En Revista: Biochimie Año: 2013 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Francia

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ribosomas / Tiouridina / Biosíntesis de Proteínas / ARN de Transferencia de Aspártico Límite: Animals / Humans Idioma: En Revista: Biochimie Año: 2013 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Francia