ArticleJournal of bacteriology2003
Genetic analysis of pathway specificity during posttranslational protein translocation across the Escherichia coli plasma membrane.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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.
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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
31 citing papers in PubMed, 74 citations in OpenAlex.
- Functional Activity of the Lysis Protein E From Phage ID52: Dependence on SecB for Efficient Host Cell Lysis.Biotechnology journal · 2026Article
- Highly efficient export of a disulfide-bonded protein to the periplasm and medium by the Tat pathway using CyDisCo in Escherichia coli.MicrobiologyOpen · 2023Article
- Exploitation of Bacillus subtilis as a robust workhorse for production of heterologous proteins and beyond.World journal of microbiology & biotechnology · 2018Review
- 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
- Signal peptides for recombinant protein secretion in bacterial expression systems.Microbial cell factories · 2018Review
- 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
- Secretome of obligate intracellular Rickettsia.FEMS microbiology reviews · 2015Review
- TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.PloS one · 2015Article
- The canonical twin-arginine translocase components are not required for secretion of folded green fluorescent protein from the ancestral strain of Bacillus subtilis.Applied and environmental microbiology · 2014Article
- Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.Journal of bacteriology · 2013Article
- Co-operation between different targeting pathways during integration of a membrane protein.The Journal of cell biology · 2012Article
- The twin-arginine translocation (Tat) protein export pathway.Nature reviews. Microbiology · 2012Review
- Twin-arginine-dependent translocation of folded proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Mapping precursor-binding site on TatC subunit of twin arginine-specific protein translocase by site-specific photo cross-linking.The Journal of biological chemistry · 2012Article
- Engineering antibody fitness and function using membrane-anchored display of correctly folded proteins.Journal of molecular biology · 2012Article
- Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB.Nature communications · 2012Article
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Escherichia coli, the SecB/SecA branch of the Sec pathway and the twin-arginine translocation (Tat) pathway represent two alternative possibilities for posttranslational translocation of proteins across the cytoplasmic membrane. Maintenance of pathway specificity was analyzed using a model precursor consisting of the mature part of the SecB-dependent maltose-binding protein (MalE) fused to the signal peptide of the Tat-dependent TorA protein. The TorA signal peptide selectively and specifically directed MalE into the Tat pathway. The characterization of a spontaneous TorA signal peptide mutant (TorA*), in which the two arginine residues in the c-region had been replaced by one leucine residue, showed that the TorA*-MalE mutant precursor had acquired the ability for efficiently using the SecB/SecA pathway. Despite the lack of the "Sec avoidance signal," the mutant precursor was still capable of using the Tat pathway, provided that the kinetically favored Sec pathway was blocked. These results show that the h-region of the TorA signal peptide is, in principle, sufficiently hydrophobic for Sec-dependent protein translocation, and therefore, the positively charged amino acid residues in the c-region represent a major determinant for Tat pathway specificity. Tat-dependent export of TorA-MalE was significantly slower in the presence of SecB than in its absence, showing that SecB can bind to this precursor despite the presence of the Sec avoidance signal in the c-region of the TorA signal peptide, strongly suggesting that the function of the Sec avoidance signal is not the prevention of SecB binding; rather, it must be exerted at a later step in the Sec pathway.
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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.