Dissecting the molecular organization of the translocon-associated protein complex

Stefan Pfeffer, Johanna Dudek, Miroslava Schaffer, Bobby G. Ng, Sahradha Albert, Jürgen M. Plitzko, Wolfgang Baumeister, Richard Zimmermann, Hudson H. Freeze, Benjamin D. Engel () and Friedrich Förster ()
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Stefan Pfeffer: Max-Planck Institute of Biochemistry
Johanna Dudek: Saarland University
Miroslava Schaffer: Max-Planck Institute of Biochemistry
Bobby G. Ng: Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute
Sahradha Albert: Max-Planck Institute of Biochemistry
Jürgen M. Plitzko: Max-Planck Institute of Biochemistry
Wolfgang Baumeister: Max-Planck Institute of Biochemistry
Richard Zimmermann: Saarland University
Hudson H. Freeze: Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute
Benjamin D. Engel: Max-Planck Institute of Biochemistry
Friedrich Förster: Max-Planck Institute of Biochemistry

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: 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.

Date: 2017
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DOI: 10.1038/ncomms14516

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