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Structure of the mammalian rescue complex with Pelota and Hbs1l assembled on a truncated mRNA.
Structural highlights
FunctionRL3_RABIT Component of the large ribosomal subunit (PubMed:26245381, PubMed:27863242). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:26245381, PubMed:27863242).[1] [2] Publication Abstract from PubMedIn 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 factorGTPase complexes representing intermediates of translation elongation (aminoacyl-tRNAeEF1A), termination (eRF1eRF3), and ribosome rescue (PelotaHbs1l). 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 factorGTPase complex to ensure translational fidelity. Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes.,Shao S, Murray J, Brown A, Taunton J, Ramakrishnan V, Hegde RS Cell. 2016 Nov 17;167(5):1229-1240.e15. doi: 10.1016/j.cell.2016.10.046. PMID:27863242[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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