ArticlePloS one2012
Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- The mechanism of Tat-dependent protein translocation.Microbial cell (Graz, Austria) · 2026Article
- Length matters: Functional flip of the short TatA transmembrane helix.Biophysical journal · 2023Article
- Bioengineering of Antibody Fragments: Challenges and Opportunities.Bioengineering (Basel, Switzerland) · 2023Review
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- Surface-exposed domains of TatB involved in the structural and functional assembly of the Tat translocase inThe Journal of biological chemistry · 2019Article
- 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
- Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide.The Journal of biological chemistry · 2017Article
- A Hinged Signal Peptide Hairpin Enables Tat-Dependent Protein Translocation.Biophysical journal · 2017Article
- How to achieve Tat transport with alien TatA.Scientific reports · 2017Article
- Article
- The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex.The Journal of biological chemistry · 2017Article
- 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
- Tracking Proteins Secreted by Bacteria: What's in the Toolbox?Frontiers in cellular and infection microbiology · 2017Review
- Assembling the Tat protein translocase.eLife · 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
- A TatABC-type Tat translocase is required for unimpaired aerobic growth of Corynebacterium glutamicum ATCC13032.PloS one · 2015Article
- TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.PloS one · 2015Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The twin arginine translocation (Tat) pathway transports folded proteins across the cytoplasmic membrane of bacteria. Tat signal peptides contain a consensus motif (S/T-R-R-X-F-L-K) that is thought to play a crucial role in substrate recognition by the Tat translocase. Replacement of the phenylalanine at the +2 consensus position in the signal peptide of a Tat-specific reporter protein (TorA-MalE) by aspartate blocked export of the corresponding TorA(D(+2))-MalE precursor, indicating that this mutation prevents a productive binding of the TorA(D(+2)) signal peptide to the Tat translocase. Mutations were identified in the extreme amino-terminal regions of TatB and TatC that synergistically suppressed the export defect of TorA(D(+2))-MalE when present in pairwise or triple combinations. The observed synergistic suppression activities were even more pronounced in the restoration of membrane translocation of another export-defective precursor, TorA(KQ)-MalE, in which the conserved twin arginine residues had been replaced by lysine-glutamine. Collectively, these findings indicate that the extreme amino-terminal regions of TatB and TatC cooperate tightly during recognition and productive binding of Tat-dependent precursor proteins and, furthermore, that TatB and TatC are both involved in the formation of a specific signal peptide binding site that reaches out as far as the end of the TatB transmembrane segment.
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