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  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., et al. (2010). Structural basis for translational stalling by human cytomegalovirus and fungal arginine attenuator peptide. doi:10.1016/j.molcel.2010.09.009.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7A24-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7A25-E
Genre: Journal Article

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 Creators:
Bhushan, S., Author
Meyer, H.1, Author              
Starosta, A. L., Author
Becker, T., Author
Mielke, T.2, Author              
Berninghausen, O., Author
Sattler, M., Author
Wilson, D. N.3, Author              
Beckmann, R., Author
Affiliations:
1In vitro Ligand Screening (Zoltán Konthur), Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479653              
2Imaging/Electron Microscopy (Head: Rudi Lurz/Thorsten Mielke), Scientific Service (Head: Manuela B. Urban), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              
3Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              

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Free keywords: Carbon-Nitrogen Ligases with Glutamine as; Amide-N-Donor/biosynthesis/chemistry/genetics; Circular Dichroism; Cryoelectron Microscopy; Cytomegalovirus/genetics/metabolism; Gene Expression Regulation, Fungal; Magnetic Resonance Spectroscopy; Models, Molecular; Nucleic Acid Conformation; Open Reading Frames; Peptide Fragments/biosynthesis/chemistry/genetics; Peptidyl Transferases/chemistry; Protein Biosynthesis; Protein Conformation; RNA, Transfer, Amino Acyl/chemistry; Ribosomal Proteins/chemistry; Ribosomes/metabolism/ultrastructure; Structure-Activity Relationship; Viral Envelope Proteins/biosynthesis/chemistry/genetics; Yeasts/genetics/metabolism
 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.

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Language(s): eng - English
 Dates: 2010-10-08
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: eDoc: 542404
DOI: 10.1016/j.molcel.2010.09.009
 Degree: -

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