ArticleScientific reports2017
Structure formation during translocon-unassisted co-translational membrane protein folding.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- The Shape of Things to Come: α-Helical Membrane Protein Folding on the Ribosome.Chemical reviews · 2026Review
- Monitoring Membrane Protein Folding Assisted by Insertases and Translocases Using AFM-Based Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- Bottom-Up Synthesis and Purification of Extracellular Vesicle Mimetics.Journal of extracellular vesicles · 2025Article
- Cell-Free Expression of Nipah Virus Transmembrane Proteins for Proteoliposome Vaccine Design.ACS nano · 2025Article
- A unifying model for membrane protein biogenesis.Nature structural & molecular biology · 2024Review
- Steric trapping strategy for studying the folding of helical membrane proteins.Methods (San Diego, Calif.) · 2024Review
- Folding speeds of helical membrane proteins.Biochemical Society transactions · 2024Review
- Dark nanodiscs for evaluating membrane protein thermostability by differential scanning fluorimetry.Biophysical journal · 2024Article
- Engineering transmembrane signal transduction in synthetic membranes using two-component systems.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Chemical Blockage of the Mitochondrial Rhomboid Protease PARL by Novel Ketoamide Inhibitors Reveals Its Role in PINK1/Parkin-Dependent Mitophagy.Journal of medicinal chemistry · 2023Article
- PEO-Biomacromolecules · 2022Article
- Three-stage model of helical membrane protein folding: Role of membrane-water interface as the intermediate stage vestibule for TM helices during their in membrano assembly.Biochemical and biophysical research communications · 2022Article
- Methods to study folding of alpha-helical membrane proteins in lipids.Open biology · 2022Review
- How lipids affect the energetics of co-translational alpha helical membrane protein folding.Biochemical Society transactions · 2022Review
- How physical forces drive the process of helical membrane protein folding.EMBO reports · 2022Review
- Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cell-Free Expression to Probe Co-Translational Insertion of an Alpha Helical Membrane Protein.Frontiers in molecular biosciences · 2022Article
- Cell-Free Membrane Protein Expression into Hybrid Lipid/Polymer Vesicles.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cell-Free Synthesis Strategies to Probe Co-translational Folding of Proteins Within Lipid Membranes.Methods in molecular biology (Clifton, N.J.) · 2022Article
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9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Correctly folded membrane proteins underlie a plethora of cellular processes, but little is known about how they fold. Knowledge of folding mechanisms centres on reversible folding of chemically denatured membrane proteins. However, this cannot replicate the unidirectional elongation of the protein chain during co-translational folding in the cell, where insertion is assisted by translocase apparatus. We show that a lipid membrane (devoid of translocase components) is sufficient for successful co-translational folding of two bacterial α-helical membrane proteins, DsbB and GlpG. Folding is spontaneous, thermodynamically driven, and the yield depends on lipid composition. Time-resolving structure formation during co-translational folding revealed different secondary and tertiary structure folding pathways for GlpG and DsbB that correlated with membrane interfacial and biological transmembrane amino acid hydrophobicity scales. Attempts to refold DsbB and GlpG from chemically denatured states into lipid membranes resulted in extensive aggregation. Co-translational insertion and folding is thus spontaneous and minimises aggregation whilst maximising correct folding.
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