ArticlePloS one2013
Efficient E. coli expression strategies for production of soluble human crystallin ALDH3A1.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 46 citations in OpenAlex.
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- Investigating the Functional Roles of Aldehyde Dehydrogenase 3A1 in Human Corneal Epithelial Cells.International journal of molecular sciences · 2023Article
- Identification of a peptide ligand for human ALDH3A1 through peptide phage display: Prediction and characterization of protein interaction sites and inhibition of ALDH3A1 enzymatic activity.Frontiers in molecular biosciences · 2023Article
- Generation of a Library of Carbohydrate-Active Enzymes for Plant Biomass Deconstruction.International journal of molecular sciences · 2022Article
- Improved production of the recombinant phospholipase A1 from3 Biotech · 2020Article
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- Identifying genomic targets for protein over-expression by "omics" analysis of Quiescent Escherichia coli cultures.Microbial cell factories · 2017Article
- Production of a Recombinant Dengue Virus 2 NS5 Protein and Potential Use as a Vaccine Antigen.Clinical and vaccine immunology : CVI · 2016Article
- Development of a high yield expression and purification system for Domain I of Beta-2-glycoprotein I for the treatment of APS.BMC biotechnology · 2015Article
- Efficient soluble expression of active recombinant human cyclin A2 mediated by E. coli molecular chaperones.Protein expression and purification · 2015Article
- Efficient in vitro refolding and functional characterization of recombinant human liver carboxylesterase (CES1) expressed in E. coli.Protein expression and purification · 2015Article
- Soluble expression of pullulanase from Bacillus acidopullulyticus in Escherichia coli by tightly controlling basal expression.Journal of industrial microbiology & biotechnology · 2014Article
- Engineering cells to improve protein expression.Current opinion in structural biology · 2014Review
- Parameters that enhance the bacterial expression of active plant polyphenol oxidases.PloS one · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aldehyde dehydrogenase 3A1 (ALDH3A1) is a recently characterized corneal crystallin with its exact functions still being unclear. Expressing recombinant human ALDH3A1 has been difficult in Escherichia coli (E. coli) because of low solubility, yield and insufficient purity issues. In this report, we compared different E. coli expression strategies (namely the maltose binding protein; MBP- and the 6-his-tagged expression systems) under conditions of auto-induction and co-expression with E. coli's molecular chaperones where appropriate. Thus, we aimed to screen the efficiency of these expression strategies in order to improve solubility of recombinant ALDH3A1 when expressed in E. coli. We showed that the MBP- tagged expression in combination with lower-temperature culture conditions resulted in active soluble recombinant ALDH3A1. Expression of the fused 6-his tagged-ALDH3A1 protein resulted in poor solubility and neither lowering temperature culture conditions nor the auto-induction strategy improved its solubility. Furthermore, higher yield of soluble, active native form of 6-his tagged-ALDH3A1 was facilitated through co-expression of the two groups of E. coli's molecular chaperones, GroES/GroEL and DnaK/DnaJ/GrpE. Convenient one step immobilized affinity chromatography methods were utilized to purify the fused ALDH3A1 hybrids. Both fusion proteins retained their biological activity and could be used directly without removing the fusion tags. Taken together, our results provide a rational option for producing sufficient amounts of soluble and active recombinant ALDH3A1 using the E. coli expression system for conducting functional studies towards elucidating the biological role(s) of this interesting corneal crystallin.
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