ArticleMethods in molecular biology (Clifton, N.J.)2022
Functional Overexpression of Membrane Proteins in E. coli: The Good, the Bad, and the Ugly.
Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 4 citations in OpenAlex.
- Evaluation of recombinant extracellular enveloped virion protein candidates for the detection of serological responses to lumpy skin disease virus in cattle.The veterinary quarterly · 2025Article
- Daptomycin avoids drug resistance mediated by the BceAB transporter inMicrobiology spectrum · 2024Article
- The transport activity of the multidrug ABC transporter BmrA does not require a wide separation of the nucleotide-binding domains.The Journal of biological chemistry · 2024Article
- Identification of a two-component regulatory system involved in antimicrobial peptide resistance in Streptococcus pneumoniae.PLoS pathogens · 2022Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Overexpression of properly folded membrane proteins is a mandatory step for their functional and structural characterization. One of the most used expression systems for the production of proteins is Escherichia coli. Many advantageous strains combined with T7 expression systems have been developed over the years. Recently, we showed that the choice of the strain is critical for the functionality of membrane proteins, even when the proteins are successfully incorporated in the membrane (Mathieu et al. Sci Rep. 2019; 9(1):2654). Notably, the amount and/or activity of the T7-RNA polymerase, which drives the transcription of the genes of interest, may indirectly affect the folding and functionality of overexpressed membrane proteins. Moreover, we reported a general trend in which mild detergents mainly extract the population of active membrane proteins, whereas a harsher detergent like Fos-choline 12 could solubilize them irrespectively of their functionality. Based on these observations, we provide some guidelines to optimize the quality of membrane proteins overexpressed in E. coli.
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