ArticleeLife2018
Dynamic action of the Sec machinery during initiation, protein translocation and termination.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Bacterial motility depends on a critical flagellum length and energy-optimized assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- AFM observation of protein translocation mediated by one unit of SecYEG-SecA complex.Nature communications · 2025Article
- The Multifunctional Preprotein Binding Domain of SecA.Chembiochem : a European journal of chemical biology · 2024Article
- SecYEG-mediated translocation in a model synthetic cell.Synthetic biology (Oxford, England) · 2024Article
- Dynamic coupling of fast channel gating with slow ATP-turnover underpins protein transport through the Sec translocon.The EMBO journal · 2024Article
- A common mechanism of Sec61 translocon inhibition by small molecules.Nature chemical biology · 2023Article
- A unifying mechanism for protein transport through the core bacterial Sec machinery.Open biology · 2023Review
- mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria.Cell reports · 2023Article
- Atomic Force Microscopy Reveals Complexity Underlying General Secretory System Activity.International journal of molecular sciences · 2022Review
- Article
- Multi-parameter photon-by-photon hidden Markov modeling.Nature communications · 2022Article
- Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022Review
- Real-time imaging of structure and dynamics of transmembrane biomolecules by FRET-induced single-molecule fluorescence attenuation.Biophysics reports · 2021Article
- Protein Export via the Type III Secretion System of the Bacterial Flagellum.Biomolecules · 2021Review
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Refined measurement of SecA-driven protein secretion reveals that translocation is indirectly coupled to ATP turnover.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs.Communications biology · 2020Article
- Comparison of Single and Multiple Turnovers of SecYEG in Escherichia coli.Journal of bacteriology · 2020Article
- Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.Nature communications · 2020Article
- Free-energy landscapes of membrane co-translocational protein unfolding.Communications biology · 2020Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Protein translocation across cell membranes is a ubiquitous process required for protein secretion and membrane protein insertion. In bacteria, this is mostly mediated by the conserved SecYEG complex, driven through rounds of ATP hydrolysis by the cytoplasmic SecA, and the trans-membrane proton motive force. We have used single molecule techniques to explore SecY pore dynamics on multiple timescales in order to dissect the complex reaction pathway. The results show that SecA, both the signal sequence and mature components of the pre-protein, and ATP hydrolysis each have important and specific roles in channel unlocking, opening and priming for transport. After channel opening, translocation proceeds in two phases: a slow phase independent of substrate length, and a length-dependent transport phase with an intrinsic translocation rate of ~40 amino acids per second for the proOmpA substrate. Broad translocation rate distributions reflect the stochastic nature of polypeptide transport.
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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.