ArticleNature2008
A role for the two-helix finger of the SecA ATPase in protein translocation.
Article in Nature, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed, 138 citations in OpenAlex.
- Review
- AFM observation of protein translocation mediated by one unit of SecYEG-SecA complex.Nature communications · 2025Article
- 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
- 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
- A unified evolutionary origin for the ubiquitous protein transporters SecY and YidC.BMC biology · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Article
- Protease protection assays show polypeptide movement into the SecY channel by power strokes of the SecA ATPase.EMBO reports · 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
- The SecA motor generates mechanical force during protein translocation.Nature communications · 2020Article
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- Structure of the substrate-engaged SecA-SecY protein translocation machine.Nature communications · 2019Article
- Direct visualization of theScience advances · 2019Article
- Protein Transport Across the Bacterial Plasma Membrane by the Sec Pathway.The protein journal · 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
- ATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinery.eLife · 2019Article
16 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
An important step in the biosynthesis of many proteins is their partial or complete translocation across the plasma membrane in prokaryotes or the endoplasmic reticulum membrane in eukaryotes. In bacteria, secretory proteins are generally translocated after completion of their synthesis by the interaction of the cytoplasmic ATPase SecA and a protein-conducting channel formed by the SecY complex. How SecA moves substrates through the SecY channel is unclear. However, a recent structure of a SecA-SecY complex raises the possibility that the polypeptide chain is moved by a two-helix finger domain of SecA that is inserted into the cytoplasmic opening of the SecY channel. Here we have used disulphide-bridge crosslinking to show that the loop at the tip of the two-helix finger of Escherichia coli SecA interacts with a polypeptide chain right at the entrance into the SecY pore. Mutagenesis demonstrates that a tyrosine in the loop is particularly important for translocation, but can be replaced by some other bulky, hydrophobic residues. We propose that the two-helix finger of SecA moves a polypeptide chain into the SecY channel with the tyrosine providing the major contact with the substrate, a mechanism analogous to that suggested for hexameric, protein-translocating ATPases.
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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.