ArticleThe EMBO journal2019
Protein translocation by the SecA ATPase occurs by a power-stroke mechanism.
Article in The EMBO journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 62 citations in OpenAlex.
- AFM observation of protein translocation mediated by one unit of SecYEG-SecA complex.Nature communications · 2025Article
- 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
- Article
- Structural basis of SecA-mediated protein translocation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Single-Molecule Optical Tweezers As a Tool for Delineating the Mechanisms of Protein-Processing Mechanoenzymes.ACS omega · 2023Review
- Atomic Force Microscopy Reveals Complexity Underlying General Secretory System Activity.International journal of molecular sciences · 2022Review
- AAA+ proteins: one motor, multiple ways to work.Biochemical Society transactions · 2022Review
- Article
- Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features.Journal of visualized experiments : JoVE · 2022Article
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- Translocation of Proteins through a Distorted Lipid Bilayer.Trends in cell biology · 2021Review
- Native-like membrane models of E. coli polar lipid extract shed light on the importance of lipid composition complexity.BMC biology · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Protease protection assays show polypeptide movement into the SecY channel by power strokes of the SecA ATPase.EMBO reports · 2020Article
- SecY-mediated quality control prevents the translocation of non-gated porins.Scientific reports · 2020Article
- Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.PLoS biology · 2020Article
- The Structure ofInternational journal of molecular sciences · 2020Article
- Interaction of the motor protein SecA and the bacterial protein translocation channel SecYEG in the absence of ATP.Nanoscale advances · 2020Article
- A single power stroke by ATP binding drives substrate translocation in a heterodimeric ABC transporter.eLife · 2020Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
SecA belongs to the large class of ATPases that use the energy of ATP hydrolysis to perform mechanical work resulting in protein translocation across membranes, protein degradation, and unfolding. SecA translocates polypeptides through the SecY membrane channel during protein secretion in bacteria, but how it achieves directed peptide movement is unclear. Here, we use single-molecule FRET to derive a model that couples ATP hydrolysis-dependent conformational changes of SecA with protein translocation. Upon ATP binding, the two-helix finger of SecA moves toward the SecY channel, pushing a segment of the polypeptide into the channel. The finger retracts during ATP hydrolysis, while the clamp domain of SecA tightens around the polypeptide, preserving progress of translocation. The clamp opens after phosphate release and allows passive sliding of the polypeptide chain through the SecA-SecY complex until the next ATP binding event. This power-stroke mechanism may be used by other ATPases that move polypeptides.
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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.