ArticleThe EMBO journal2010
Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported.
Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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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
29 citing papers in PubMed.
- Transport of Folded Proteins by the Tat System.The protein journal · 2019Review
- The Twin-Arginine Pathway for Protein Secretion.EcoSal Plus · 2019Review
- 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
- Precursor-Receptor Interactions in the Twin Arginine Protein Transport Pathway Probed with a New Receptor Complex Preparation.Biochemistry · 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
- PvdN Enzyme Catalyzes a Periplasmic Pyoverdine Modification.The Journal of biological chemistry · 2016Article
- TatE as a Regular Constituent of Bacterial Twin-arginine Protein Translocases.The Journal of biological chemistry · 2015Article
- 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
- Initial assembly steps of a translocase for folded proteins.Nature communications · 2015Article
- Reconstruction and modeling protein translocation and compartmentalization in Escherichia coli at the genome-scale.BMC systems biology · 2014Article
- Substrate-gated docking of pore subunit Tha4 in the TatC cavity initiates Tat translocase assembly.The Journal of cell biology · 2014Article
- Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Mapping the signal peptide binding and oligomer contact sites of the core subunit of the pea twin arginine protein translocase.The Plant cell · 2013Article
- Intra-plastid protein trafficking: how plant cells adapted prokaryotic mechanisms to the eukaryotic condition.Biochimica et biophysica acta · 2013Review
- Direct interaction between a precursor mature domain and transport component Tha4 during twin arginine transport of chloroplasts.Plant physiology · 2013Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The thylakoid twin arginine protein translocation (Tat) system is thought to have a multivalent receptor complex with each cpTatC-Hcf106 pair constituting a signal peptide-binding unit. Conceptual models suggest that translocation of individual precursor proteins occurs upon assembly of a Tha4 oligomer with a precursor-occupied cpTatC-Hcf106. However, results reported here reveal that multiple precursor proteins bound to a single receptor complex can be transported together. Precursor proteins that contain one or two cysteine residues readily formed intermolecular disulphide bonds upon binding to the receptor complex, resulting in dimeric and tetrameric precursor proteins. Three lines of evidence indicate that all members of precursor oligomers were specifically bound to a receptor unit. Blue native-polyacrylamide gel electrophoresis analysis showed that oligomers were present on individual receptor complexes rather than bridging two or more receptor complexes. Upon energizing the membrane, the dimeric and tetrameric precursors were transported across the membrane with efficiencies comparable with that of monomeric precursors. These results imply a novel aspect of Tat systems, whereby multiple precursor-binding sites can act in concert to transport an interlinked oligo-precursor protein.
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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.