ArticlemBio2017
Signal Peptide Hydrophobicity Modulates Interaction with the Twin-Arginine Translocase.
Article in mBio, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Review
- The Transmembrane Glutamate Serves as a pH Sensor for Tha4 Oligomerization During Twin Arginine Transport of Proteins.Plants (Basel, Switzerland) · 2025Article
- Signal Peptides: From Molecular Mechanisms to Applications in Protein and Vaccine Engineering.Biomolecules · 2025Review
- Heterologous protein exposure and secretion optimization in Mycoplasma pneumoniae.Microbial cell factories · 2024Article
- Identification of novel tail-anchored membrane proteins integrated by the bacterial twin-arginine translocase.Microbiology (Reading, England) · 2024Article
- Characterization of a TatA/TatB binding site on the TatC component of theMicrobiology (Reading, England) · 2023Article
- Analysis of the Brucella suis Twin Arginine Translocation System and Its Substrates Shows That It Is Essential for Viability.Infection and immunity · 2023Article
- The biogenesis of β-lactamase enzymes.Microbiology (Reading, England) · 2022Review
- An Engineered Outer Membrane-DefectiveJournal of microbiology and biotechnology · 2022Article
- Article
- The Tat system and its dependent cell division proteins are critical for virulence of extra-intestinal pathogenicVirulence · 2020Article
- Targeting of proteins to the twin-arginine translocation pathway.Molecular microbiology · 2020Review
- Tat-Dependent Heterologous Secretion of Recombinant Tyrosinase by Pseudomonas fluorescens Is Aided by a Translationally Fused Caddie Protein.Applied and environmental microbiology · 2019Article
- Surface-exposed domains of TatB involved in the structural and functional assembly of the Tat translocase inThe Journal of biological chemistry · 2019Article
- Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries.Heliyon · 2019Article
- Routing of thylakoid lumen proteins by the chloroplast twin arginine transport pathway.Photosynthesis research · 2018Review
- Evolution of mitochondrial TAT translocases illustrates the loss of bacterial protein transport machines in mitochondria.BMC biology · 2018Article
- Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018Article
- Genome wide identification and experimental validation of Pseudomonas aeruginosa Tat substrates.Scientific reports · 2018Article
- The early mature part of bacterial twin-arginine translocation (Tat) precursor proteins contributes to TatBC receptor binding.The Journal of biological chemistry · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The general secretory pathway (Sec) and twin-arginine translocase (Tat) operate in parallel to export proteins across the cytoplasmic membrane of prokaryotes and the thylakoid membrane of plant chloroplasts. Substrates are targeted to their respective machineries by N-terminal signal peptides that share a tripartite organization; however, Tat signal peptides harbor a conserved and almost invariant arginine pair that is critical for efficient targeting to the Tat machinery. Tat signal peptides interact with a membrane-bound receptor complex comprised of TatB and TatC components, with TatC containing the twin-arginine recognition site. Here, we isolated suppressors in the signal peptide of the Tat substrate, SufI, that restored Tat transport in the presence of inactivating substitutions in the TatC twin-arginine binding site. These suppressors increased signal peptide hydrophobicity, and copurification experiments indicated that they restored binding to the variant TatBC complex. The hydrophobic suppressors could also act in
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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.