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          Institute: MPI für molekulare Genetik     Collection: Department of Vertebrate Genomics     Display Documents

ID: 542404.0, MPI für molekulare Genetik / Department of Vertebrate Genomics
Structural basis for translational stalling by human cytomegalovirus and fungal arginine attenuator peptide
Authors:Bhushan, S.; Meyer, H.; Starosta, A. L.; Becker, T.; Mielke, T.; Berninghausen, O.; Sattler, M.; Wilson, D. N.; Beckmann, R.
Date of Publication (YYYY-MM-DD):2010-10-08
Copyright:© 2010 Elsevier B.V.
Audience:Experts Only
Abstract / Description: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.
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
Comment of the Author/Creator:Correspondence: wilson@lmb.uni-muenchen.de (D.N.W.), beckmann@lmb.uni-muenchen.de (R.B.)
External Publication Status:published
Document Type:Article
Communicated by:Hans Lehrach
Affiliations:MPI für molekulare Genetik
External Affiliations:Gene Center and Department of Biochemistry and Center for integrated Protein Science Munich, University of Munich,
Feodor-Lynen-Strasse 25, 81377 Munich, Germany
Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany
Munich Center for Integrated Protein Science at Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany
Institut für Medizinische Physik und Biophysik, Charité , Ziegelstrasse 5-8, 10117 Berlin, Germany
Identifiers:ISSN:1097-4164 (Electronic) [ID No:1]
DOI:10.1016/j.molcel.2010.09.009 [ID No:2]
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