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Exploring the molecular composition of the multipass translocon in its native membrane environment
Open accessPreprint — published as 10.26508/lsa.202302496
Abstract
Multispanning membrane proteins are inserted into the endoplasmic reticulum membrane by the ribosome-bound multipass translocon machinery. Based on cryo-electron tomography and extensive subtomogram analysis, we reveal the composition and arrangement of multipass translocon components in their native membrane environment. The intramembrane chaperone complex PAT and the translocon associated protein (TRAP) complex associate substoichiometrically with the multipass translocon in a translation-dependent manner. While PAT is preferentially recruited to active complexes, TRAP primarily associates with inactive translocons. The subtomogram average of the TRAP-multipass translocon reveals intermolecular contacts between the luminal domains of TRAP and an unknown subunit of the BOS complex. AlphaFold modeling suggests this protein is NOMO, bridging the luminal domains of nicalin and TRAPα. Collectively, our results visualize the interplay of accessory factors associated with multipass membrane protein biogenesis under near-native conditions.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Gemmer, M., Chaillet, M. L., & Förster, F.
- Affiliations
- Utrecht University (NL)
- Corresponding author
- Förster, Friedrich
- Venue
- Life Science Alliance
- Publisher
- openRxiv
- Published
- 2023-11-29
- Volume
- 7
- Issue
- 8
- Pages
- e202302496-e202302496
- ISSN
- 2575-1077 (ISSN-L)
- PMC
- PMC11169918
- OpenAlex
- W4399566271
- Cited by
- 16
- References
- 1
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 4 · 2023: 1
- FWCI
- 2.04
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Life Science Alliance (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Funders
- European Commission (724425, HORIZON2020)
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (724.016.001, 184.034.014, 724.016.001, 184.034.014, 741.018.201, 741.018.201)
- European Research Council (724425)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- endoplasmic reticulum membrane, TRAP complex, Sec61, protein translocation, membrane protein insertion, cryo-electron tomography, protein complex composition
- MeSH terms
- SEC Translocation Channels, Endoplasmic Reticulum, Membrane Proteins, Models, Molecular, Ribosomes, Protein Biosynthesis, Molecular Chaperones, Cryoelectron Microscopy, Protein Transport
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