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Modulation of translational decoding by m6A modification of mRNA.
Jain, Sakshi; Koziej, Lukasz; Poulis, Panagiotis; Kaczmarczyk, Igor; Gaik, Monika; Rawski, Michal; Ranjan, Namit; Glatt, Sebastian; Rodnina, Marina V.
Afiliación
  • Jain S; Max Planck Institute for Multidisciplinary Sciences, Göttingen, 37077, Germany.
  • Koziej L; Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, 30-387, Poland.
  • Poulis P; Max Planck Institute for Multidisciplinary Sciences, Göttingen, 37077, Germany.
  • Kaczmarczyk I; Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, 30-387, Poland.
  • Gaik M; Doctoral School of Exact and Natural Sciences, Jagiellonian University, Krakow, 30-387, Poland.
  • Rawski M; Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, 30-387, Poland.
  • Ranjan N; Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, 30-387, Poland.
  • Glatt S; National Synchrotron Radiation Centre SOLARIS, Jagiellonian University, Krakow, 30-387, Poland.
  • Rodnina MV; Max Planck Institute for Multidisciplinary Sciences, Göttingen, 37077, Germany.
Nat Commun ; 14(1): 4784, 2023 08 08.
Article en En | MEDLINE | ID: mdl-37553384
N6-methyladenosine (m6A) is an abundant, dynamic mRNA modification that regulates key steps of cellular mRNA metabolism. m6A in the mRNA coding regions inhibits translation elongation. Here, we show how m6A modulates decoding in the bacterial translation system using a combination of rapid kinetics, smFRET and single-particle cryo-EM. We show that, while the modification does not impair the initial binding of aminoacyl-tRNA to the ribosome, in the presence of m6A fewer ribosomes complete the decoding process due to the lower stability of the complexes and enhanced tRNA drop-off. The mRNA codon adopts a π-stacked codon conformation that is remodeled upon aminoacyl-tRNA binding. m6A does not exclude canonical codon-anticodon geometry, but favors alternative more dynamic conformations that are rejected by the ribosome. These results highlight how modifications outside the Watson-Crick edge can still interfere with codon-anticodon base pairing and complex recognition by the ribosome, thereby modulating the translational efficiency of modified mRNAs.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Biosíntesis de Proteínas / Anticodón Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2023 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Biosíntesis de Proteínas / Anticodón Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2023 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido