ArticleScientific reports2018
A novel regulation mechanism of the T7 RNA polymerase based expression system improves overproduction and folding of membrane proteins.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 61 citations in OpenAlex.
- Innovations, Challenges and Future Directions of T7RNA Polymerase in Microbial Cell Factories.ACS synthetic biology · 2025Review
- Deciphering Transcription-Translation-Folding (TX-TL-FD) for Enhancing Cutinase Production in T7 System and Genetic Chaperone-EquippedACS synthetic biology · 2025Article
- Fine-tuning the yeast GAL10 promoter and growth conditions for efficient recombinant membrane protein production and purification.Protein science : a publication of the Protein Society · 2025Article
- Essential factors, advanced strategies, challenges, and approaches involved for efficient expression of recombinant proteins in Escherichia coli.Archives of microbiology · 2024Review
- Escherichia coli strains with precise domain deletions in the ribonuclease RNase E can achieve greatly enhanced levels of membrane protein production.Protein science : a publication of the Protein Society · 2024Article
- Efficient stereoselective hydroxylation of deoxycholic acid by the robust whole-cell cytochrome P450 CYP107D1 biocatalyst.Synthetic and systems biotechnology · 2023Article
- Whole-Cell P450 Biocatalysis Using Engineered Escherichia coli with Fine-Tuned Heme Biosynthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Plasmids for Controlled and Tunable High-Level Expression in E. coli.Applied and environmental microbiology · 2022Article
- Second-GenerationACS synthetic biology · 2022Article
- High-throughput cell-free screening of eukaryotic membrane protein expression in lipidic mimetics.Protein science : a publication of the Protein Society · 2022Article
- Membrane Protein Production in Escherichia coli: Protocols and Rules.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Functional Overexpression of Membrane Proteins in E. coli: The Good, the Bad, and the Ugly.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The high-throughput production of membrane proteins.Emerging topics in life sciences · 2021Article
- Targetron-Assisted Delivery of Exogenous DNA Sequences intoACS synthetic biology · 2021Article
- A plasmid toolbox for controlled gene expression across the Proteobacteria.Nucleic acids research · 2021Article
- Protein over-expression in Escherichia coli triggers adaptation analogous to antimicrobial resistance.Microbial cell factories · 2021Article
- Changes in Membrane Protein Structural Biology.Biology · 2020Review
- Inducible intracellular membranes: molecular aspects and emerging applications.Microbial cell factories · 2020Review
- Escherichia coli σMicrobial cell factories · 2020Article
- Shaping the lipid composition of bacterial membranes for membrane protein production.Microbial cell factories · 2019Article
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Authors and funding
10 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane protein (MP) overproduction is one of the major bottlenecks in structural genomics and biotechnology. Despite the emergence of eukaryotic expression systems, bacteria remain a cost effective and powerful tool for protein production. The T7 RNA polymerase (T7RNAP)-based expression system is a successful and efficient expression system, which achieves high-level production of proteins. However some foreign MPs require a fine-tuning of their expression to minimize the toxicity associated with their production. Here we report a novel regulation mechanism for the T7 expression system. We have isolated two bacterial hosts, namely C44(DE3) and C45(DE3), harboring a stop codon in the T7RNAP gene, whose translation is under the control of the basal nonsense suppressive activity of the BL21(DE3) host. Evaluation of hosts with superfolder green fluorescent protein (sfGFP) revealed an unprecedented tighter control of transgene expression with a marked accumulation of the recombinant protein during stationary phase. Analysis of a collection of twenty MP fused to GFP showed an improved production yield and quality of several bacterial MPs and of one human monotopic MP. These mutant hosts are complementary to the other existing T7 hosts and will increase the versatility of the T7 expression system.
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