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  Dissecting the molecular organization of the translocon-associated protein complex

Pfeffer, S., Dudek, J., Schaffer, M., Ng, B. G., Albert, S., Plitzko, J. M., et al. (2017). Dissecting the molecular organization of the translocon-associated protein complex. Nature Communications, 8: 14516. doi:10.1038/ncomms14516.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-DD79-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-DD7A-2
Genre: Journal Article

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 Creators:
Pfeffer, Stefan1, Author              
Dudek, Johanna2, Author
Schaffer, Miroslava1, Author              
Ng, Bobby G.2, Author
Albert, Sahradha1, Author              
Plitzko, Jürgen M.1, Author              
Baumeister, Wolfgang1, Author              
Zimmermann, Richard2, Author
Freeze, Hudson H.2, Author
Engel, Benjamin D.1, Author              
Förster, Friedrich1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

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Free keywords: SIGNAL-SEQUENCE RECEPTOR; ENDOPLASMIC-RETICULUM MEMBRANE; IN-SITU; CRYOELECTRON TOMOGRAPHY; SEC61 TRANSLOCON; ER MEMBRANE; CRYO-EM; RIBOSOME; TRAP; RESOLUTIONScience & Technology - Other Topics;
 Abstract: In eukaryotic cells, one-third of all proteins must be transported across or inserted into the endoplasmic reticulum (ER) membrane by the ER protein translocon. The translocon-associated protein (TRAP) complex is an integral component of the translocon, assisting the Sec61 protein-conducting channel by regulating signal sequence and transmembrane helix insertion in a substrate-dependent manner. Here we use cryo-electron tomography (CET) to study the structure of the native translocon in evolutionarily divergent organisms and disease-linked TRAP mutant fibroblasts from human patients. The structural differences detected by subtomogram analysis form a basis for dissecting the molecular organization of the TRAP complex. We assign positions to the four TRAP subunits within the complex, providing insights into their individual functions. The revealed molecular architecture of a central translocon component advances our understanding of membrane protein biogenesis and sheds light on the role of TRAP in human congenital disorders of glycosylation.

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Language(s): eng - English
 Dates: 2017-02-20
 Publication Status: Published online
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000394457600001
DOI: 10.1038/ncomms14516
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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 8 Sequence Number: 14516 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723