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Open Access Green as soon as Postprint is submitted to ZB.
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
e-ISSN
1097-4164
Journal
Molecular Cell
Quellenangaben
Volume: 40,
Issue: 1,
Pages: 138-146
Publisher
Elsevier
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)