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Título: | Structural basis for the transition from translation initiation to elongation by an 80S-eIF5B complex |
Autor: | Wang, Jinfan; Wang, Jing; Shin, Byung-Sik; Kim, Joo-Ran; Dever, Thomas E.; Puglisi, Joseph D.; Sánchez Fernández, Israel | Palabras clave: | Cryoelectron microscopy Ribosome RNA tRNAs |
Fecha de publicación: | 2020 | Editor: | Springer Nature | Citación: | Nature Communications 11: 5003 (2020) | Resumen: | Recognition of a start codon by the initiator aminoacyl-tRNA determines the reading frame of messenger RNA (mRNA) translation by the ribosome. In eukaryotes, the GTPase eIF5B collaborates in the correct positioning of the initiator Met-tRNAiMet on the ribosome in the later stages of translation initiation, gating entrance into elongation. Leveraging the long residence time of eIF5B on the ribosome recently identified by single-molecule fluorescence measurements, we determine the cryoEM structure of the naturally long-lived ribosome complex with eIF5B and Met-tRNAiMet immediately before transition into elongation. The structure uncovers an unexpected, eukaryotic specific and dynamic fidelity checkpoint implemented by eIF5B in concert with components of the large ribosomal subunit. | Descripción: | © The Author(s) 2020. | Versión del editor: | http://dx.doi.org/10.1038/s41467-020-18829-3 | URI: | http://hdl.handle.net/10261/241440 | DOI: | 10.1038/s41467-020-18829-3 | E-ISSN: | 2041-1723 |
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Structural_Wang_PV_Art2020.pdf | 3,32 MB | Adobe PDF | Visualizar/Abrir |
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