ArticleThe EMBO journal2007
Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 148 citations in OpenAlex.
- AFM observation of protein translocation mediated by one unit of SecYEG-SecA complex.Nature communications · 2025Article
- Characterization of membrane protein interactions by peptidisc-mediated mass photometry.iScience · 2024Article
- Recent advances in membrane mimetics for membrane protein research.Biochemical Society transactions · 2023Review
- Uncovering the Optimal Molecular Characteristics of Hydrophobe-Containing Polypeptoids to Induce Liposome or Cell Membrane Fragmentation.Biomacromolecules · 2023Article
- Characterization of a soluble library of themicroLife · 2023Article
- Current Developments in Native Nanometric Discoidal Membrane Bilayer Formed by Amphipathic Polymers.Nanomaterials (Basel, Switzerland) · 2021Review
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Co-translational insertion and topogenesis of bacterial membrane proteins monitored in real time.The EMBO journal · 2020Article
- Cardiolipin is required in vivo for the stability of bacterial translocon and optimal membrane protein translocation and insertion.Scientific reports · 2020Article
- Article
- A snapshot of membrane protein insertion.EMBO reports · 2019Article
- Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.mBio · 2019Article
- Investigating the stability of the SecA-SecYEG complex during protein translocation across the bacterial membrane.The Journal of biological chemistry · 2019Article
- Dynamic Water Hydrogen-Bond Networks at the Interface of a Lipid Membrane Containing Palmitoyl-Oleoyl Phosphatidylglycerol.The Journal of membrane biology · 2018Article
- Nanodiscs: A Controlled Bilayer Surface for the Study of Membrane Proteins.Annual review of biophysics · 2018Article
- Human P450 CYP17A1: Control of Substrate Preference by Asparagine 202.Biochemistry · 2018Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017Review
- Article
- A method for detergent-free isolation of membrane proteins in their local lipid environment.Nature protocols · 2016Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The translocon is a membrane-embedded protein assembly that catalyzes protein movement across membranes. The core translocon, the SecYEG complex, forms oligomers, but the protein-conducting channel is at the center of the monomer. Defining the properties of the SecYEG protomer is thus crucial to understand the underlying function of oligomerization. We report here the reconstitution of a single SecYEG complex into nano-scale lipid bilayers, termed Nanodiscs. These water-soluble particles allow one to probe the interactions of the SecYEG complex with its cytosolic partner, the SecA dimer, in a membrane-like environment. The results show that the SecYEG complex triggers dissociation of the SecA dimer, associates only with the SecA monomer and suffices to (pre)-activate the SecA ATPase. Acidic lipids surrounding the SecYEG complex also contribute to the binding affinity and activation of SecA, whereas mutations in the largest cytosolic loop of the SecY subunit, known to abolish the translocation reaction, disrupt both the binding and activation of SecA. Altogether, the results define the fundamental contribution of the SecYEG protomer in the translocation subreactions and illustrate the power of nanoscale lipid bilayers in analyzing the dynamics occurring at the membrane.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.