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



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ID: 307710.0, MPI für molekulare Genetik / Department of Vertebrate Genomics
Signal recognition particle receptor exposes the ribosomal translocon binding site
Authors:Halic, Mario; Gartmann, Marco; Schlenker, Oliver; Mielke, Thorsten; Pool, Martin R.; Sinning, Irmgard; Beckmann, Roland
Language:English
Date of Publication (YYYY-MM-DD):2006-05-05
Title of Journal:Science
Volume:312
Issue / Number:5774
Start Page:745
End Page:747
Copyright:© 2006 American Association for the Advancement of Science
Review Status:not specified
Audience:Experts Only
Abstract / Description:Signal sequences of secretory and membrane proteins are recognized by the signal recognition particle (SRP) as they emerge from the ribosome. This results in their targeting to the membrane by docking with the SRP receptor, which facilitates transfer of the ribosome to the translocon. Here, we present the 8 angstrom cryo–electron microscopy structure of a "docking complex" consisting of a SRP-bound 80S ribosome and the SRP receptor. Interaction of the SRP receptor with both SRP and the ribosome rearranged the S domain of SRP such that a ribosomal binding site for the translocon, the L23e/L35 site, became exposed, whereas Alu domain–mediated elongation arrest persisted.
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:Institute of Biochemistry, Charité, University Medical School Berlin, Monbijoustrasse 2, 10117 Berlin, Germany;
Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany;
University of Manchester, Faculty of Life Sciences, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK
Identifiers:ISSN:0036-8075
DOI:10.1126/science.1124864
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