PuSH - Publication Server of Helmholtz Zentrum München

Bhushan, S.* ; Meyer, H. ; Starosta, A.L.* ; Becker, T.* ; Mielke, T.* ; Berninghausen, O.* ; Sattler, M. ; Wilson, D.N.* ; Beckmann, R.*

Structural basis for translational stalling by human cytomegalovirus and fungal arginine attenuator peptide.

Mol. Cell 40, 138-146 (2010)
DOI Order publishers version
Open Access Green as soon as Postprint is submitted to ZB.
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.
Altmetric
Additional Metrics?
Edit extra informations Login
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 Article Number: , Supplement: ,
Publisher Elsevier
Reviewing status Peer reviewed