ArticleThe Journal of biological chemistry2017
The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Signal peptide engineering of a novel M4 family keratinase and the action mechanism in promoting pepper tolerance to salt stress through KerJY23-hydrolyzed feather waste.Synthetic and systems biotechnology · 2026Article
- Signal Peptides: From Molecular Mechanisms to Applications in Protein and Vaccine Engineering.Biomolecules · 2025Review
- Advancements in Escherichia coli secretion systems for enhanced recombinant protein production.World journal of microbiology & biotechnology · 2025Review
- Targeting of proteins to the twin-arginine translocation pathway.Molecular microbiology · 2020Review
- Cross-Species Functional Conservation and Possible Origin of the N-Terminal Specificity Domain of Mitochondrial Presequences.Frontiers in plant science · 2020Article
- 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
- 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
- Precursor-Receptor Interactions in the Twin Arginine Protein Transport Pathway Probed with a New Receptor Complex Preparation.Biochemistry · 2018Article
- 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
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The twin-arginine translocation (Tat) pathway transports folded proteins across bacterial membranes. Tat precursor proteins possess a conserved twin-arginine (RR) motif in their signal peptides that is involved in their binding to the Tat translocase, but some facets of this interaction remain unclear. Here, we investigated the role of the hydrophobic (h-) region of the
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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.