ArticleMicrobial biotechnology2008
Exploration of twin-arginine translocation for expression and purification of correctly folded proteins in Escherichia coli.
Article in Microbial biotechnology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 30 citations in OpenAlex.
- Two-Tiered Selection and Screening Strategy to Increase Functional Enzyme Production in E. coli.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Electrochromic shift supports the membrane destabilization model of Tat-mediated transport and shows ion leakage during Sec transport.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- Selection of High Producers From Combinatorial Libraries for the Production of Recombinant Proteins inFrontiers in bioengineering and biotechnology · 2019Article
- Periscope: quantitative prediction of soluble protein expression in the periplasm of Escherichia coli.Scientific reports · 2016Article
- Modified recombinant proteins can be exported via the Sec pathway in Escherichia coli.PloS one · 2012Article
- Production of secretory and extracellular N-linked glycoproteins in Escherichia coli.Applied and environmental microbiology · 2011Article
- Versatile selection technology for intracellular protein-protein interactions mediated by a unique bacterial hitchhiker transport mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Environmental Microbiology meets Microbial Biotechnology.Microbial biotechnology · 2008Article
- Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Historically, the general secretory (Sec) pathway of Gram-negative bacteria has served as the primary route by which heterologous proteins are delivered to the periplasm in numerous expression and engineering applications. Here we have systematically examined the twin-arginine translocation (Tat) pathway as an alternative, and possibly advantageous, secretion pathway for heterologous proteins. Overall, we found that: (i) export efficiency and periplasmic yield of a model substrate were affected by the composition of the Tat signal peptide, (ii) Tat substrates were correctly processed at their N-termini upon reaching the periplasm and (iii) proteins fused to maltose-binding protein (MBP) were reliably exported by the Tat system, but only when correctly folded; aberrantly folded MBP fusions were excluded by the Tat pathway's folding quality control feature. We also observed that Tat export yield was comparable to Sec for relatively small, well-folded proteins, higher relative to Sec for proteins that required cytoplasmic folding, and lower relative to Sec for larger, soluble fusion proteins. Interestingly, the specific activity of material purified from the periplasm was higher for certain Tat substrates relative to their Sec counterparts, suggesting that Tat expression can give rise to relatively pure and highly active proteins in one step.
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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.