ArticleMolecular biology of the cell2009
Clustering of C-terminal stromal domains of Tha4 homo-oligomers during translocation by the Tat protein transport system.
Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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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.
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Who cites it
42 citing papers in PubMed, 65 citations in OpenAlex.
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- The mechanism of Tat-dependent protein translocation.Microbial cell (Graz, Austria) · 2026Article
- 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
- Occurrence and potential mechanism of holin-mediated non-lytic protein translocation in bacteria.Microbial cell (Graz, Austria) · 2022Review
- 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
- 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
- The Tat protein transport system: intriguing questions and conundrums.FEMS microbiology letters · 2018Review
- The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane ofThe Journal of biological chemistry · 2018Article
- Unanticipated functional diversity among the TatA-type components of the Tat protein translocase.Scientific reports · 2018Article
- Prolines in Transit Peptides Are Crucial for Efficient Preprotein Translocation into Chloroplasts.Plant physiology · 2018Article
- Engineered Cross-Linking to Study the Pore Architecture of the CRAC Channel.Methods in molecular biology (Clifton, N.J.) · 2018Article
- A Hinged Signal Peptide Hairpin Enables Tat-Dependent Protein Translocation.Biophysical journal · 2017Article
- Article
- A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.Molecular microbiology · 2015Article
- Mechanistic Aspects of Folded Protein Transport by the Twin Arginine Translocase (Tat).The Journal of biological chemistry · 2015Review
- TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.PloS one · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The chloroplast Twin arginine translocation (Tat) pathway uses three membrane proteins and the proton gradient to transport folded proteins across sealed membranes. Precursor proteins bind to the cpTatC-Hcf106 receptor complex, triggering Tha4 assembly and protein translocation. Tha4 is required only for the translocation step and is thought to be the protein-conducting component. The organization of Tha4 oligomers was examined by substituting pairs of cysteine residues into Tha4 and inducing disulfide cross-links under varying stages of protein translocation. Tha4 formed tetramers via its transmembrane domain in unstimulated membranes and octamers in membranes stimulated by precursor and the proton gradient. Tha4 formed larger oligomers of at least 16 protomers via its carboxy tail, but such C-tail clustering only occurred in stimulated membranes. Mutational studies showed that transmembrane domain directed octamers as well as C-tail clusters require Tha4's transmembrane glutamate residue and its amphipathic helix, both of which are necessary for Tha4 function. A novel double cross-linking strategy demonstrated that both transmembrane domain directed- and C-tail directed oligomerization occur in the translocase. These results support a model in which Tha4 oligomers dock with a precursor-receptor complex and undergo a conformational switch that results in activation for protein transport. This possibly involves accretion of additional Tha4 into a larger transport-active homo-oligomer.
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Registered trials
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