Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes

By S. Shao, J. Murray, Alan Brown, J. Taunton, V. Ramakrishnan, R. Hegde. 2016

226 citations recorded by the source corpus.

Summary 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.

Subfields: Molecular Biology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

Citations in the corpus

Mechanisms that ensure speed and fidelity in eukaryotic translation termination (2021, background): “Right, posttermination (modeled by 40S alignment, PDB IDs: 5LZU and 3J77 (14, 37)).”
Long-range interdomain communications in eIF5B regulate GTP hydrolysis and translation initiation (2020, background): “Other mechanisms, especially in the larger, more complex mammalian ribosomes, operate in a similar logic (4): multidomain protein factors recognize a specific state of the ribosome, and if certain criteria are met, a signal is propagated and amplified by the coupling of the ribosomal movements with ”