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



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ID: 542341.0, MPI für molekulare Genetik / Department of Vertebrate Genomics
alpha-Helical nascent polypeptide chains visualized within distinct regions of the ribosomal exit tunnel
Authors:Bhushan, S.; Gartmann, M.; Halic, M.; Armache, J. P.; Jarasch, A.; Mielke, T.; Berninghausen, O.; Wilson, D. N.; Beckmann, R.
Language:English
Date of Publication (YYYY-MM-DD):2010-03
Title of Journal:Nature Structural & Molecular Biology
Journal Abbrev.:Nat Struct Mol Biol
Volume:17
Issue / Number:3
Start Page:313
End Page:317
Copyright:© 2010 Nature Publishing Group
Review Status:not specified
Audience:Experts Only
Abstract / Description:As translation proceeds, the nascent polypeptide chain passes through a tunnel in the large ribosomal subunit. Although this ribosomal exit tunnel was once thought only to be a passive conduit for the growing nascent chain, accumulating evidence suggests that it may in fact play a more active role in regulating translation and initial protein folding events. Here we have determined single-particle cryo-electron microscopy reconstructions of eukaryotic 80S ribosomes containing nascent chains with high alpha-helical propensity located within the exit tunnel. The maps enable direct visualization of density for helices as well as allowing the sites of interaction with the tunnel wall components to be elucidated. In particular regions of the tunnel, the nascent chain adopts distinct conformations and establishes specific contacts with tunnel components, both ribosomal RNA and proteins, that have been previously implicated in nascent chain-ribosome interaction.
Free Keywords:Computer Simulation; Cryoelectron Microscopy; Image Processing, Computer-Assisted; Models, Biological; Peptides/chemistry/metabolism; Protein Biosynthesis; Protein Conformation; Protein Folding; Ribosomes/chemistry/metabolism/ultrastructure
Comment of the Author/Creator:email: beckmann@lmb.uni-muenchen.de
External Publication Status:published
Document Type:Article
Communicated by:Hans Lehrach
Affiliations:MPI für molekulare Genetik
External Affiliations:Gene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany
Institut für Medizinische Physik und Biophysik, Charité, Berlin, Germany
Identifiers:ISSN:1545-9985 (Electronic) [ID No:1]
DOI:10.1038/nsmb.1756 [ID No:2]
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