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-Structure paper
Title | Structural basis for the transition from translation initiation to elongation by an 80S-eIF5B complex. |
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Journal, issue, pages | Nat Commun, Vol. 11, Issue 1, Page 5003, Year 2020 |
Publish date | Oct 6, 2020 |
Authors | Jinfan Wang / Jing Wang / Byung-Sik Shin / Joo-Ran Kim / Thomas E Dever / Joseph D Puglisi / Israel S Fernández / |
PubMed Abstract | 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 ...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-tRNA 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-tRNA 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. |
External links | Nat Commun / PubMed:33024099 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.9 Å |
Structure data | EMDB-21859, PDB-6woo: |
Chemicals | ChemComp-ZN: ChemComp-GDP: ChemComp-U6A: ChemComp-MET: |
Source |
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Keywords | RIBOSOME / yeast / initiation / eIF5B / GDP / Met-tRNAiMet |