Structure of the mammalian oligosaccharyl-transferase complex in the native ER protein translocon

Stefan Pfeffer, Johanna Dudek, Marko Gogala, Stefan Schorr, Johannes Linxweiler, Sven Lang, Thomas Becker, Roland Beckmann, Richard Zimmermann and Friedrich Förster ()
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Stefan Pfeffer: Max-Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany
Johanna Dudek: Saarland University
Marko Gogala: Gene Center and Center for integrated Protein Science Munich, University of Munich
Stefan Schorr: Saarland University
Johannes Linxweiler: Saarland University
Sven Lang: Saarland University
Thomas Becker: Gene Center and Center for integrated Protein Science Munich, University of Munich
Roland Beckmann: Gene Center and Center for integrated Protein Science Munich, University of Munich
Richard Zimmermann: Saarland University
Friedrich Förster: Max-Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany

Nature Communications, 2014, vol. 5, issue 1, 1-8

Abstract: Abstract In mammalian cells, proteins are typically translocated across the endoplasmic reticulum (ER) membrane in a co-translational mode by the ER protein translocon, comprising the protein-conducting channel Sec61 and additional complexes involved in nascent chain processing and translocation. As an integral component of the translocon, the oligosaccharyl-transferase complex (OST) catalyses co-translational N-glycosylation, one of the most common protein modifications in eukaryotic cells. Here we use cryoelectron tomography, cryoelectron microscopy single-particle analysis and small interfering RNA-mediated gene silencing to determine the overall structure, oligomeric state and position of OST in the native ER protein translocon of mammalian cells in unprecedented detail. The observed positioning of OST in close proximity to Sec61 provides a basis for understanding how protein translocation into the ER and glycosylation of nascent proteins are structurally coupled. The overall spatial organization of the native translocon, as determined here, serves as a reliable framework for further hypothesis-driven studies.

Date: 2014
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DOI: 10.1038/ncomms4072

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