ArticleProceedings of the National Academy of Sciences of the United States of America2014
Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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78 citing papers in PubMed, 145 citations in OpenAlex.
- The Shape of Things to Come: α-Helical Membrane Protein Folding on the Ribosome.Chemical reviews · 2026Review
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Off-target structural insights: ArnA and AcrB in bacterial membrane-protein cryo-EM analysis.Acta crystallographica. Section D, Structural biology · 2025Article
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- The versatile role of YidC in membrane protein biosynthesis and quality control.Biochimica et biophysica acta. Molecular cell research · 2025Review
- Functional diversity and molecular interactions of small membrane proteins in bacteria.microLife · 2025Review
- Deciphering the Interdomain Coupling in a Gram-Negative Bacterial Membrane Insertase.The journal of physical chemistry. B · 2024Article
- Whole Cell Luminescence-Based Screen for Inhibitors of the Bacterial Sec Machinery.Biochemistry · 2024Article
- Chemiosmotic nutrient transport in synthetic cells powered by electrogenic antiport coupled to decarboxylation.Nature communications · 2024Article
- Steric trapping strategy for studying the folding of helical membrane proteins.Methods (San Diego, Calif.) · 2024Review
- Dynamic coupling of fast channel gating with slow ATP-turnover underpins protein transport through the Sec translocon.The EMBO journal · 2024Article
- YidC fromBiomolecules · 2023Article
- The insertase YidC chaperones the polytopic membrane protein MelB inserting and folding simultaneously from both termini.Structure (London, England : 1993) · 2023Article
- TerC proteins function during protein secretion to metalate exoenzymes.Nature communications · 2023Article
- Uncovering the Important Genetic Factors for Growth during Cefotaxime-Gentamicin Combination Treatment inAntibiotics (Basel, Switzerland) · 2023Article
- TerC Proteins Function During Protein Secretion to Metalate Exoenzymes.Research square · 2023Article
- TerC Proteins Function During Protein Secretion to Metalate Exoenzymes.bioRxiv : the preprint server for biology · 2023Article
- Interaction of the periplasmic chaperone SurA with the inner membrane protein secretion (SEC) machinery.The Biochemical journal · 2023Article
- Genome-wide CRISPRi screen identifies enhanced autolithotrophic phenotypes in acetogenic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2023Article
18 more citing papers are in PubMed but not listed here.
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11 authors at 4 institutions in 2 countries.
Funding
Abstract
The SecY/61 complex forms the protein-channel component of the ubiquitous protein secretion and membrane protein insertion apparatus. The bacterial version SecYEG interacts with the highly conserved YidC and SecDF-YajC subcomplex, which facilitates translocation into and across the membrane. Together, they form the holo-translocon (HTL), which we have successfully overexpressed and purified. In contrast to the homo-dimeric SecYEG, the HTL is a hetero-dimer composed of single copies of SecYEG and SecDF-YajC-YidC. The activities of the HTL differ from the archetypal SecYEG complex. It is more effective in cotranslational insertion of membrane proteins and the posttranslational secretion of a β-barreled outer-membrane protein driven by SecA and ATP becomes much more dependent on the proton-motive force. The activity of the translocating copy of SecYEG may therefore be modulated by association with different accessory subcomplexes: SecYEG (forming SecYEG dimers) or SecDF-YajC-YidC (forming the HTL). This versatility may provide a means to refine the secretion and insertion capabilities according to the substrate. A similar modularity may also be exploited for the translocation or insertion of a wide range of substrates across and into the endoplasmic reticular and mitochondrial membranes of eukaryotes.
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