ArticleBMC biotechnology2007
Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli.
Article in BMC biotechnology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.
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Who cites it
114 citing papers in PubMed.
- A generalizable method for the purification and biophysical characterization of bacterial membrane receptors.Protein science : a publication of the Protein Society · 2026Article
- A Novel Recombinant MAGE-B10-HSP110 Fusion Protein Enhances Innate and Adaptive Immune Responses in Mice: A Potential Vaccine Candidate for Canine Mammary Tumors.Animals : an open access journal from MDPI · 2026Article
- Computational optimization of DEK1 calpain domain solubility through integrated structural modelling and data-driven targeted mutagenesis.Scientific reports · 2026Article
- A biosensor toolbox for monitoring recombinant protein production inFrontiers in bioengineering and biotechnology · 2026Article
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- High-Throughput Pipeline for Protein Expression and Solubility Profiling Using Synthetically Generated Plasmids.Current protocols · 2025Article
- Bacillus subtilis surface display technology: applications in bioprocessing and sustainable manufacturing.Biotechnology for biofuels and bioproducts · 2025Review
- A review on computational models for predicting protein solubility.Journal of microbiology (Seoul, Korea) · 2025Review
- The molecular dissection of TRIM25's RNA-binding mechanism provides key insights into its antiviral activity.Nature communications · 2024Article
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- Bacterial Production of CDKL5 Catalytic Domain: Insights in Aggregation, Internal Translation and Phosphorylation Patterns.International journal of molecular sciences · 2024Article
- Plant Heat Shock Proteins Are More Effective in Enhancing Recombinant Alcohol Dehydrogenase Activity than Bacterial OnesIranian journal of biotechnology · 2024Article
- Arabidopsis metacaspase MC1 localizes in stress granules, clears protein aggregates, and delays senescence.The Plant cell · 2023Article
- Review
- Expression and Purification of Glycosyltransferase DnmS fromMicroorganisms · 2023Article
- Essential mitochondrial role in iron-sulfur cluster assembly of the cytoplasmic isopropylmalate isomerase Leu1 in Saccharomyces cerevisiae.Mitochondrion · 2023Article
- Synthesis of an Anti-CD7 Recombinant Immunotoxin Based on PE24 in CHO andInternational journal of molecular sciences · 2022Article
- GroEL-A Versatile Chaperone for Engineering and a Plethora of Applications.Biomolecules · 2022Review
- Comparative expression of soluble, active human kinases in specialized bacterial strains.PloS one · 2022Article
- Co-Expression of Chaperones for Improvement of Soluble Expression and Purification of An Anti-HER2 scFv inAdvanced biomedical research · 2022Article
54 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe overproduction of recombinant proteins in host cells often leads to their misfolding and aggregation. Previous attempts to increase the solubility of recombinant proteins by co-overproduction of individual chaperones were only partially successful. We now assessed the effects of combined overproduction of the functionally cooperating chaperone network of the E. coli cytosol on the solubility of recombinant proteins.
resultsA two-step procedure was found to show the strongest enhancement of solubility. In a first step, the four chaperone systems GroEL/GroES, DnaK/DnaJ/GrpE, ClpB and the small HSPs IbpA/IbpB, were coordinately co-overproduced with recombinant proteins to optimize de novo folding. In a second step, protein biosynthesis was inhibited to permit chaperone mediated refolding of misfolded and aggregated proteins in vivo. This novel strategy increased the solubility of 70% of 64 different heterologous proteins tested up to 42-fold.
conclusionThe engineered E. coli strains and the two-step procedure presented here led to a remarkable increase in the solubility of a various recombinant proteins and should be applicable to a wide range of target proteins produced in biotechnology.
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