Structure of the mammalian oligosaccharyl-transferase complex in the native ER protein translocon
| Autor: | Thomas Becker, Friedrich Förster, Stefan Schorr, Roland Beckmann, Stefan Pfeffer, Sven Lang, Johanna Dudek, Richard Zimmermann, Marko Gogala, Johannes Linxweiler |
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| Rok vydání: | 2014 |
| Předmět: |
Sec61
Glycosylation General Physics and Astronomy Biology Endoplasmic Reticulum Transferase complex General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound N-linked glycosylation Humans Gene Silencing RNA Small Interfering Cells Cultured Multidisciplinary Endoplasmic reticulum membrane Endoplasmic reticulum Cryoelectron Microscopy Membrane Proteins General Chemistry Translocon Cell biology Protein Transport Hexosyltransferases chemistry lipids (amino acids peptides and proteins) SEC Translocation Channels HeLa Cells Transcription Factors |
| Zdroj: | Nature Communications. 5 |
| ISSN: | 2041-1723 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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