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

ID: 456467.0, MPI für molekulare Genetik / Department of Vertebrate Genomics
Structure of Monomeric Yeast and Mammalian Sec61 Complexes Interacting with the Translating Ribosome.
Authors:Becker, Thomas; Bhushan, Shashi; Jarasch, Alexander; Armache, Jean-Paul; Soledad, Soledad; Jossinet, Fabrice; Gumbart, James; Mielke, Thorsten; Berninghausen, Otto; Schulten, Klaus; Westhof, Eric; Gilmore, Reid; Mandon, Elisabet C.; Beckmann, Roland
Date of Publication (YYYY-MM-DD):2009-12-04
Title of Journal:Science
Journal Abbrev.:Science
Issue / Number:5958
Start Page:1369
End Page:1373
Copyright:2009 by the American Association for the Advancement of Science; all rights reserved. The title Science is a
American Association for the Advancement of Science, 1200 New York Avenue NW, Washington, DC 20005.
Review Status:not specified
Audience:Experts Only
Abstract / Description:The trimeric Sec61/SecY complex is a protein-conducting channel (PCC) for secretory and membrane proteins. Although Sec complexes can form oligomers, it has been suggested that a single copy may serve as an active PCC. We determined subnanometer-resolution cryo–electron microscopy structures of eukaryotic ribosome-Sec61 complexes. In combination with biochemical data, we found that in both idle and active states, the Sec complex is not oligomeric and interacts mainly via two cytoplasmic loops with the universal ribosomal adaptor site. In the active state, the ribosomal tunnel and a central pore of the monomeric PCC were occupied by the nascent chain, contacting loop 6 of the Sec complex. This provides a structural basis for the activity of a solitary Sec complex in cotranslational protein translocation.
Comment of the Author/Creator:To whom correspondence should be addressed.
E-mail: (E.M.); (R.B.)
External Publication Status:published
Document Type:Article
Communicated by:Hans Lehrach
Affiliations:MPI für molekulare Genetik
External Affiliations:1.Gene Center Munich and Center for Integrated Protein Science, Department of Chemistry and Biochemistry, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany;
2.Departamento de Bioquímica, Instituto de Fisiología Celular, Circuito Exterior s/n, Ciudad Universitaria, Universidad Nacional Autónoma de México, Mexico, Distrito Federal, 04510, Mexico;
3.Institut de Biologie Moléculaire et Cellulaire du CNRS, Architecture et Réactivité de l’ARN, Université de Strasbourg, 15 rue René Descartes, F-67084 Strasbourg, France;
4.Department of Physics, Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA;
5.Institut für Medizinische Physik und Biophysik, Charite–Universitätsmedizin Berlin, Ziegelstrasse 5-9, 10117-Berlin, Germany;
6.Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605, USA.
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