ArticleThe Journal of cell biology2012
Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complex.
Article in The Journal of cell biology, 2012. 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.
- Dynamic coupling of fast channel gating with slow ATP-turnover underpins protein transport through the Sec translocon.The EMBO journal · 2024Article
- A unifying mechanism for protein transport through the core bacterial Sec machinery.Open biology · 2023Review
- Structural basis of SecA-mediated protein translocation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Article
- 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
- Interaction of the motor protein SecA and the bacterial protein translocation channel SecYEG in the absence of ATP.Nanoscale advances · 2020Article
- Capturing Membrane Protein Ribosome Nascent Chain Complexes in a Native-like Environment for Co-translational Studies.Biochemistry · 2020Article
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- Crosslinking and Reconstitution Approaches to Study Protein Transport.The protein journal · 2019Review
- Protein translocation by the SecA ATPase occurs by a power-stroke mechanism.The EMBO journal · 2019Article
- Investigating the stability of the SecA-SecYEG complex during protein translocation across the bacterial membrane.The Journal of biological chemistry · 2019Article
- Substrate Proteins Take Shape at an Improved Bacterial Translocon.Journal of bacteriology · 2019Article
- Dynamic action of the Sec machinery during initiation, protein translocation and termination.eLife · 2018Article
- The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.FEMS microbiology letters · 2018Review
- The SecA protein deeply penetrates into the SecYEG channel during insertion, contacting most channel transmembrane helices and periplasmic regions.The Journal of biological chemistry · 2017Article
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Alignment of the protein substrate hairpin along the SecA two-helix finger primes protein transport inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The bacterial ATPase SecA and protein channel complex SecYEG form the core of an essential protein translocation machinery. The nature of the conformational changes induced by each stage of the hydrolytic cycle of ATP and how they are coupled to protein translocation are not well understood. The structure of the SecA-SecYEG complex revealed a 2-helix-finger (2HF) of SecA in an ideal position to contact the substrate protein and push it through the membrane. Surprisingly, immobilization of this finger at the edge of the protein channel had no effect on translocation, whereas its imposition inside the channel blocked transport. This analysis resolves the stoichiometry of the active complex, demonstrating that after the initiation process translocation requires only one copy each of SecA and SecYEG. The results also have important implications on the mechanism of energy transduction and the power stroke driving transport. Evidently, the 2HF is not a highly mobile transducing element of polypeptide translocation.
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Registered trials
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