ArticleThe Journal of cell biology2001
Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport.
Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.
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Who cites it
112 citing papers in PubMed.
- Structure and substrate recognition by the bacterial twin-arginine translocation (Tat) core complex.Nature microbiology · 2026Article
- Sensing and Filtering Environmental Fluctuations: The Case of Biomolecular Condensates in Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- The Transmembrane Glutamate Serves as a pH Sensor for Tha4 Oligomerization During Twin Arginine Transport of Proteins.Plants (Basel, Switzerland) · 2025Article
- A larger TatBC complex associates with TatA clusters for transport of folded proteins across the bacterial cytoplasmic membrane.Scientific reports · 2024Article
- Length matters: Functional flip of the short TatA transmembrane helix.Biophysical journal · 2023Article
- New insights into the Tat protein transport cycle from characterizing the assembled Tat translocon.Molecular microbiology · 2022Article
- Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex.Communications biology · 2022Article
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- Evolution of an assembly factor-based subunit contributed to a novel NDH-PSI supercomplex formation in chloroplasts.Nature communications · 2021Article
- Electrochromic shift supports the membrane destabilization model of Tat-mediated transport and shows ion leakage during Sec transport.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- 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
- 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
- Evolution of mitochondrial TAT translocases illustrates the loss of bacterial protein transport machines in mitochondria.BMC biology · 2018Article
- Tat-exported peptidoglycan amidase-dependent cell division contributes to Salmonella Typhimurium fitness in the inflamed gut.PLoS pathogens · 2018Article
- Thylakoid-integrated recombinant Hcf106 participates in the chloroplast twin arginine transport system.Plant direct · 2018Article
- The Tat protein transport system: intriguing questions and conundrums.FEMS microbiology letters · 2018Review
52 more citing papers are in PubMed but not listed here.
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2 authors.
Funding
Abstract
The thylakoid DeltapH-dependent pathway transports folded proteins with twin arginine-containing signal peptides. Identified components of the machinery include cpTatC, Hcf106, and Tha4. The reaction occurs in two steps: precursor binding to the machinery, and transport across the membrane. Here, we show that a cpTatC-Hcf106 complex serves as receptor for specific binding of twin arginine-containing precursors. Antibodies to either Hcf106 or cpTatC, but not Tha4, inhibited precursor binding. Blue native gel electrophoresis and coimmunoprecipitation of digitonin-solubilized thylakoids showed that Hcf106 and cpTatC are members of an approximately 700-kD complex that lacks Tha4. Thylakoid-bound precursor proteins were also associated with an approximately 700-kD complex and were coimmunoprecipitated with antibodies to cpTatC or Hcf106. Chemical cross-linking revealed that precursors make direct contact with cpTatC and Hcf106 and confirmed that Tha4 is not associated with precursor, cpTatC, or Hcf106 in the membrane. Precursor binding to the cpTatC-Hcf106 complex required both the twin arginine and the hydrophobic core of the signal peptide. Precursors remained bound to the complex when Tha4 was sequestered by antibody, even in the presence of DeltapH. These results indicate that precursor binding to the cpTatC-Hcf106 complex constitutes the recognition event for this pathway and that subsequent participation by Tha4 leads to translocation.
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