ArticleThe Journal of biological chemistry2007
Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 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.
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Who cites it
63 citing papers in PubMed, 129 citations in OpenAlex.
- Review
- Insights into the proteome of next-generation probiotic Faecalibacterium duncaniae A2-165 through label-free proteomics approach.BMC microbiology · 2026Article
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- Identification of novel tail-anchored membrane proteins integrated by the bacterial twin-arginine translocase.Microbiology (Reading, England) · 2024Article
- Highly efficient export of a disulfide-bonded protein to the periplasm and medium by the Tat pathway using CyDisCo in Escherichia coli.MicrobiologyOpen · 2023Article
- Signal Peptide Efficiency: From High-Throughput Data to Prediction and Explanation.ACS synthetic biology · 2023Article
- Analysis of the Brucella suis Twin Arginine Translocation System and Its Substrates Shows That It Is Essential for Viability.Infection and immunity · 2023Article
- Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella.Microbiology spectrum · 2022Article
- The biogenesis of β-lactamase enzymes.Microbiology (Reading, England) · 2022Review
- Article
- Twin-arginine translocation (Tat) mutants inFEMS microbes · 2021Article
- 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
- Escherichia coli "TatExpress" strains export several g/L human growth hormone to the periplasm by the Tat pathway.Biotechnology and bioengineering · 2019Article
- Transport of Folded Proteins by the Tat System.The protein journal · 2019Review
- The Twin-Arginine Pathway for Protein Secretion.EcoSal Plus · 2019Review
- Plasma-sensitive Escherichia coli mutants reveal plasma resistance mechanisms.Journal of the Royal Society, Interface · 2019Article
- Mutagenesis-Based Characterization and Improvement of a Novel Inclusion Body Tag.Frontiers in bioengineering and biotechnology · 2019Article
- Selection of High Producers From Combinatorial Libraries for the Production of Recombinant Proteins inFrontiers in bioengineering and biotechnology · 2019Article
- Exploitation of Bacillus subtilis as a robust workhorse for production of heterologous proteins and beyond.World journal of microbiology & biotechnology · 2018Review
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The Escherichia coli genome encodes at least 29 putative signal peptides containing a twin arginine motif characteristic of proteins exported via the twin arginine translocation (Tat) pathway. Fusions of the putative Tat signal peptides plus six to eight amino acids of the mature proteins to three reporter proteins (short-lived green fluorescent protein, maltose-binding protein (MBP), and alkaline phosphatase) and also data from the cell localization of epitope-tagged full-length proteins were employed to determine the ability of the 29 signal peptides to direct export through the Tat pathway, through the general secretory pathway (Sec), or through both. 27/29 putative signal peptides could export one or more reporter proteins through Tat. Of these, 11 signal peptides displayed Tat specificity in that they could not direct the export of Sec-only reporter proteins. The rest (16/27) were promiscuous and were capable of directing export of the appropriate reporter either via Tat (green fluorescent protein, MBP) or via Sec (PhoA, MBP). Mutations that conferred a >or=+1 charge to the N terminus of the mature protein abolished or drastically reduced routing through the Sec pathway without affecting the ability to export via the Tat pathway. These experiments demonstrate that the charge of the mature protein N terminus affects export promiscuity, independent of the effect of the folding state of the mature protein.
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What OpenQuestion holds
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.