ArticleThe Journal of biological chemistry2014
Ion conductivity of the bacterial translocation channel SecYEG engaged in translocation.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The trial behind it
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Who cites it
15 citing papers in PubMed.
- Functional mapping and engineering of the Sec translocon unlocked by a cell-free system.Science advances · 2026Article
- YidC fromBiomolecules · 2023Article
- Determinants of Lipid Domain Size.International journal of molecular sciences · 2022Article
- Biophysical Reviews' "Meet the Councilor Series"-a profile of Peter Pohl.Biophysical reviews · 2021Article
- Structural determinants of a permeation barrier of the SecYEG translocon in the active state.Physical chemistry chemical physics : PCCP · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Comparison of Single and Multiple Turnovers of SecYEG in Escherichia coli.Journal of bacteriology · 2020Article
- Interaction of the motor protein SecA and the bacterial protein translocation channel SecYEG in the absence of ATP.Nanoscale advances · 2020Article
- Voltage Sensing in Bacterial Protein Translocation.Biomolecules · 2020Article
- AFM-Based Force Spectroscopy Guided by Recognition Imaging: A New Mode for Mapping and Studying Interaction Sites at Low Lateral Density.Methods and protocols · 2019Article
- Driving Forces of Translocation Through Bacterial Translocon SecYEG.The Journal of membrane biology · 2018Article
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- YidC and SecYEG form a heterotetrameric protein translocation channel.Scientific reports · 2017Article
- Tuning membrane protein mobility by confinement into nanodomains.Nature nanotechnology · 2017Article
- Energy coupling mechanisms of MFS transporters.Protein science : a publication of the Protein Society · 2015Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
While engaged in protein transport, the bacterial translocon SecYEG must maintain the membrane barrier to small ions. The preservation of the proton motif force was attributed to (i) cation exclusion, (ii) engulfment of the nascent chain by the hydrophobic pore ring, and (iii) a half-helix partly plugging the channel. In contrast, we show here that preservation of the proton motif force is due to a voltage-driven conformational change. Preprotein or signal peptide binding to the purified and reconstituted SecYEG results in large cation and anion conductivities only when the membrane potential is small. Physiological values of membrane potential close the activated channel. This voltage-dependent closure is not dependent on the presence of the plug domain and is not affected by mutation of 3 of the 6 constriction residues to glycines. Cellular ion homeostasis is not challenged by the small remaining leak conductance.
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Registered trials
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