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Structural basis for translational stalling by human cytomegalovirus and fungal arginine attenuator peptide.
Mol. Cell 40, 138-146 (2010)
Specific regulatory nascent chains establish direct interactions with the ribosomal tunnel, leading to translational stalling. Despite a wealth of biochemical data, structural insight into the mechanism of translational stalling in eukaryotes is still lacking. Here we use cryo-electron microscopy to visualize eukaryotic ribosomes stalled during the translation of two diverse regulatory peptides: the fungal arginine attenuator peptide (AAP) and the human cytomegalovirus (hCMV) gp48 upstream open reading frame 2 (uORF2). The C terminus of the AAP appears to be compacted adjacent to the peptidyl transferase center (PTC). Both nascent chains interact with ribosomal proteins L4 and L17 at tunnel constriction in a distinct fashion. Significant changes at the PTC were observed: the eukaryotic-specific loop of ribosomal protein L10e establishes direct contact with the CCA end of the peptidyl-tRNA (P-tRNA), which may be critical for silencing of the PTC during translational stalling. Our findings provide direct structural insight into two distinct eukaryotic stalling processes.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Open reading frame; Ribosome; RNA; Inhibition; Tunnel; System; Tools; Gene
ISSN (print) / ISBN 1097-2765
Journal Molecular Cell
Quellenangaben Volume: 40, Issue: 1, Pages: 138-146
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)