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

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

doi:10.1016/j.molcel.2010.09.009

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

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Meyer, H.
In vitro Ligand Screening (Zoltán Konthur), Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Mielke, T.
Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Wilson, D. N.
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Citation

Bhushan, S., Meyer, H., Starosta, A. L., Becker, T., Mielke, T., Berninghausen, O., et al. (2010). Structural basis for translational stalling by human cytomegalovirus and fungal arginine attenuator peptide. doi:10.1016/j.molcel.2010.09.009.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-7A24-0

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 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.