ArticleThe Journal of cell biology2002
A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid [Delta]pH/Tat translocase.
Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
80 citing papers in PubMed.
- Structure and substrate recognition by the bacterial twin-arginine translocation (Tat) core complex.Nature microbiology · 2026Article
- Review
- The Transmembrane Glutamate Serves as a pH Sensor for Tha4 Oligomerization During Twin Arginine Transport of Proteins.Plants (Basel, Switzerland) · 2025Article
- Characterization of a TatA/TatB binding site on the TatC component of theMicrobiology (Reading, England) · 2023Article
- New insights into the Tat protein transport cycle from characterizing the assembled Tat translocon.Molecular microbiology · 2022Article
- Recognition of discrete export signals in early flagellar subunits during bacterial type III secretion.eLife · 2022Article
- The ten amino acids of the oxygen-evolving enhancer of tobacco is sufficient as the peptide residues for protein transport to the chloroplast thylakoid.Plant molecular biology · 2021Article
- Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.PloS one · 2021Article
- Targeting of proteins to the twin-arginine translocation pathway.Molecular microbiology · 2020Review
- Surface-exposed domains of TatB involved in the structural and functional assembly of the Tat translocase inThe Journal of biological chemistry · 2019Article
- Transport of Folded Proteins by the Tat System.The protein journal · 2019Review
- The Twin-Arginine Pathway for Protein Secretion.EcoSal Plus · 2019Review
- A Potential Late Stage Intermediate of Twin-Arginine Dependent Protein Translocation inFrontiers in microbiology · 2019Article
- Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway.Photosynthesis research · 2018Review
- Thylakoid-integrated recombinant Hcf106 participates in the chloroplast twin arginine transport system.Plant direct · 2018Article
- Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018Article
- The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane ofThe Journal of biological chemistry · 2018Article
- The early mature part of bacterial twin-arginine translocation (Tat) precursor proteins contributes to TatBC receptor binding.The Journal of biological chemistry · 2018Article
- Signal peptides for recombinant protein secretion in bacterial expression systems.Microbial cell factories · 2018Review
- Unanticipated functional diversity among the TatA-type components of the Tat protein translocase.Scientific reports · 2018Article
20 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
The thylakoid DeltapH-dependent/Tat pathway is a novel system with the remarkable ability to transport tightly folded precursor proteins using a transmembrane DeltapH as the sole energy source. Three known components of the transport machinery exist in two distinct subcomplexes. A cpTatC-Hcf106 complex serves as precursor receptor and a Tha4 complex is required after precursor recognition. Here we report that Tha4 assembles with cpTatC-Hcf106 during the translocation step. Interactions among components were examined by chemical cross-linking of intact thylakoids followed by immunoprecipitation and immunoblotting. cpTatC and Hcf106 were consistently associated under all conditions tested. In contrast, Tha4 was only associated with cpTatC and Hcf106 in the presence of a functional precursor and the DeltapH. Interestingly, a synthetic signal peptide could replace intact precursor in triggering assembly. The association of all three components was transient and dissipated upon the completion of protein translocation. Such an assembly-disassembly cycle could explain how the DeltapH/Tat system can assemble translocases to accommodate folded proteins of varied size. It also explains in part how the system can exist in the membrane without compromising its ion and proton permeability barrier.
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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.