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-Structure paper
Title | Structural basis for translational stalling by human cytomegalovirus and fungal arginine attenuator peptide. |
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Journal, issue, pages | Mol Cell, Vol. 40, Issue 1, Page 138-146, Year 2010 |
Publish date | Oct 8, 2010 |
Authors | Shashi Bhushan / Helge Meyer / Agata L Starosta / Thomas Becker / Thorsten Mielke / Otto Berninghausen / Michael Sattler / Daniel N Wilson / Roland Beckmann / |
PubMed Abstract | 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 ...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. |
External links | Mol Cell / PubMed:20932481 |
Methods | EM (single particle) / NMR (solution) |
Resolution | 6.5 - 6.7 Å |
Structure data | EMDB-1767: EMDB-1768: PDB-2xl1: |
Source |
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Keywords | TRANSLATION / ANTIBIOTIC / RIBOSOME / CYTOMEGALOVIRUS |