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Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes.

Shao S, Murray J, Brown A, Taunton J, Ramakrishnan V, Hegde RS
Cell 167 1229-1240.e15 (2016)
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Cited: 106 times
EuropePMC logo PMID: 27863242

Abstract

In eukaryotes, accurate protein synthesis relies on a family of translational GTPases that pair with specific decoding factors to decipher the mRNA code on ribosomes. We present structures of the mammalian ribosome engaged with decoding factor⋅GTPase complexes representing intermediates of translation elongation (aminoacyl-tRNA⋅eEF1A), termination (eRF1⋅eRF3), and ribosome rescue (Pelota⋅Hbs1l). Comparative analyses reveal that each decoding factor exploits the plasticity of the ribosomal decoding center to differentially remodel ribosomal proteins and rRNA. This leads to varying degrees of large-scale ribosome movements and implies distinct mechanisms for communicating information from the decoding center to each GTPase. Additional structural snapshots of the translation termination pathway reveal the conformational changes that choreograph the accommodation of decoding factors into the peptidyl transferase center. Our results provide a structural framework for how different states of the mammalian ribosome are selectively recognized by the appropriate decoding factor⋅GTPase complex to ensure translational fidelity.

Articles - 5lzx mentioned but not cited (2)

  1. Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes. Shao S, Murray J, Brown A, Taunton J, Ramakrishnan V, Hegde RS. Cell 167 1229-1240.e15 (2016)
  2. Functionally distinct roles for eEF2K in the control of ribosome availability and p-body abundance. Smith PR, Loerch S, Kunder N, Stanowick AD, Lou TF, Campbell ZT. Nat Commun 12 6789 (2021)


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