ArticleThe Journal of biological chemistry2012
Kinetics of precursor interactions with the bacterial Tat translocase detected by real-time FRET.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- The mechanism of Tat-dependent protein translocation.Microbial cell (Graz, Austria) · 2026Article
- Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex.Communications biology · 2022Article
- Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.PloS one · 2021Article
- 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
- High Throughput Screen for Escherichia coli Twin Arginine Translocation (Tat) Inhibitors.PloS one · 2016Article
- 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
- Co-factor insertion and disulfide bond requirements for twin-arginine translocase-dependent export of the Bacillus subtilis Rieske protein QcrA.The Journal of biological chemistry · 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
- Choreography of importin-α/CAS complex assembly and disassembly at nuclear pores.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Effect of cargo size and shape on the transport efficiency of the bacterial Tat translocase.FEBS letters · 2013Article
- The twin-arginine translocation (Tat) protein export pathway.Nature reviews. Microbiology · 2012Review
- Stoichiometry for binding and transport by the twin arginine translocation system.The Journal of cell biology · 2012Article
- Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB.Nature communications · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The Escherichia coli twin-arginine translocation (Tat) system transports fully folded and assembled proteins across the inner membrane into the periplasmic space. Traditionally, in vitro protein translocation studies have been performed using gel-based transport assays. This technique suffers from low time resolution, and often, an inability to distinguish between different steps in a continuously occurring translocation process. To address these limitations, we have developed an in vitro FRET-based assay that reports on an early step in the Tat translocation process in real-time. The natural Tat substrate pre-SufI was labeled with Alexa532 (donor), and the fluorescent protein mCherry (acceptor) was fused to the C terminus of TatB or TatC. The colored Tat proteins were easily visible during purification, enabling identification of a highly active inverted membrane vesicle (IMV) fraction yielding transport rates with NADH almost an order of magnitude faster than previously reported. When pre-SufI was bound to the translocon, FRET was observed for both Tat proteins. FRET was diminished upon addition of nonfluorescent pre-SufI, indicating that the initial binding step is reversible. When the membranes were energized with NADH, the FRET signal was lost after a short delay. These data suggest a model in which a Tat cargo initially associates with the TatBC complex, and an electric field gradient is required for the cargo to proceed to the next stage of transport. This cargo migration away from the TatBC complex requires a significant fraction of the total transport time.
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