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



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ID: 307700.0, MPI für molekulare Genetik / Department of Vertebrate Genomics
Following the signal sequence from ribosomal tunnel exit to signal recognition particle
Authors:Halic, Mario; Blau, Michael; Becker, Thomas; Mielke, Thorsten; Pool, Martin R.; Wild, Klemens; Sinning, Irmgard; Beckmann, Roland
Language:English
Date of Publication (YYYY-MM-DD):2006-11-23
Title of Journal:Nature
Volume:444
Issue / Number:7118
Start Page:507
End Page:511
Copyright:© 2007 Nature Publishing Group
Review Status:not specified
Audience:Experts Only
Abstract / Description:Membrane and secretory proteins can be co-translationally inserted into or translocated across the membrane. This process is dependent on signal sequence recognition on the ribosome by the signal recognition particle (SRP), which results in targeting of the ribosome–nascent-chain complex to the protein-conducting channel at the membrane. Here we present an ensemble of structures at subnanometre resolution, revealing the signal sequence both at the ribosomal tunnel exit and in the bacterial and eukaryotic ribosome–SRP complexes. Molecular details of signal sequence interaction in both prokaryotic and eukaryotic complexes were obtained by fitting high-resolution molecular models. The signal sequence is presented at the ribosomal tunnel exit in an exposed position ready for accommodation in the hydrophobic groove of the rearranged SRP54 M domain. Upon ribosome binding, the SRP54 NG domain also undergoes a conformational rearrangement, priming it for the subsequent docking reaction with the NG domain of the SRP receptor. These findings provide the structural basis for improving our understanding of the early steps of co-translational protein sorting.
Comment of the Author/Creator:e-mail: 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, Department of Chemistry and Biochemistry, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany;
UltraStructureNetwork, USN, Max Planck Institute for Molecular Genetics, Ihnestrasse 63–73, 14195 Berlin, Germany;
Faculty of Life Sciences, Michael Smith Building, University of Manchester, Oxford Road, Manchester M13 9PT, UK;
Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
Identifiers:ISSN:0028-0836
DOI:10.1038/nature05326
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