Aug 2026· Synthetic and Systems Biotechnology· Vol 17, pp. 144 - 154· 0 citations· 53 references
Medicine
TL;DR
Findings support the use of selective pressure to reduce recombinant expression heterogeneity and suppress low-expression subpopulations and highlight the potential use of d-serine and similar toxic substrates to simultaneously function as selective agents, inducers, and sources of essential metabolites through detoxification.
Abstract
In this work, selective pressure was applied in E. coli to enrich the population expressing recombinant proteins and suppress the emergence of low-expression phenotypes. To this end, plasmids were constructed containing two reporter genes, a degradable green fluorescent protein (GFP) and a stable red fluorescent protein (RFP), positioned upstream of either a gentamicin acetyltransferase gene or a d-serine deaminase gene. Flow cytometry analysis revealed that gentamicin selection prevented the formation of bimodal populations and maintained predominantly homogeneous expression profiles, accompanied by up to 12-fold and 10-fold increases in RFP and GFP fluorescence, respectively. These results suggest that selective pressure favoured the enrichment and maintenance of highly expressing phenotypes while preserving operon functionality. Transcriptomic analysis indicated extensive physiological adaptation under gentamicin selection, including changes in translation-related functions and increased transcript abundance of the genes of interest. To establish an antibiotic-free strategy, d-serine was employed as an alternative selective agent. Detoxification of d-serine by d-serine deaminase similarly reduced population heterogeneity and resulted in predominantly single-expression populations with up to 4-fold and 6-fold higher RFP and GFP fluorescence, respectively. Furthermore, d-serine was evaluated as the sole nitrogen source, combining selective pressure with an auxotrophic strategy and yielding up to 6-fold and 15-fold increases in RFP and GFP fluorescence, respectively. These findings support the use of selective pressure to reduce recombinant expression heterogeneity and suppress low-expression subpopulations. Additionally, we highlighted the potential use of d-serine and similar toxic substrates to simultaneously function as selective agents, inducers, and sources of essential metabolites through detoxification.
This review summarizes recent advances in engineering key expression elements underlying heterologous protein production in K. phaffii, with particular emphasis on promoter architecture redesign, signal peptide replacement and sequence engineering, molecular chaperone co-expression, and quantitative regulation of the unfolded protein response.
Ru-Yue Han, Ruizheng Hu, An-Ran Liu et al.· Journal of Fungi· 1 citation
A previous study demonstrated that quorum sensing (QS) genes from the psychrophilic bacterium Aliivibrio logei can be used in Escherichia coli to obtain bacterial cultures with controlled amounts of a target protein. However, the QS system may be induced non-uniformly across the cell population. In this study, we used an expression vector containing luxR/luxI regulatory genes from A. logei carrying sfGFP as a reporter gene. Reporter expression was regulated by the autoinducer 3OxoC6-HSL, activated at 22 °C, and terminated at 37 °C. Flow cytometry was used to assess the GFP fluorescence distribution at the single-cell level. The system provided dose-dependent unimodal expression lacking formation of distinct ON/OFF subpopulations, while the robust coefficient of variation decreased with increasing autoinducer concentration. The autoinducer synthase LuxI enabled autoinduction, but under the tested conditions, no substantial effect on expression homogeneity was detected. Raising the temperature to 37 °C effectively halted expression, allowing intermediate target protein values to be fixed at the single-cell level. Overall, the developed system represents a promising tool for biotechnological applications requiring precise and uniform control of expression.
E. Scheglova, Sabina Nebieva, K. Mekhantseva et al.· BioTech· 0 citations
Gene-programmable expression element library is rapidly expanding, making the regulation of key genes increasingly convenient. A temperature biosensor system was constructed to utilize environmental temperature conditions for gene expression regulation, thereby reducing reliance on costly chemical inducers and enabling successful application to product synthesis. Existing biosensors based on the temperature response of CI857-PR have shortcomings, which greatly limit their application. In this study, we constructed a dual-dependent promoter library P38X for σ70 and σ38 and combined it with the operator gene R1 in the PR promoter to achieve structural decoupling from the wild-type PR promoter and improve promoter persistence in the stationary phase. The method was successfully applied to the de novo lycopene synthesis in Escherichia coli, obtaining a final yield of 116 mg/L within 48 h under shake-flask fermentation. Protein degradation tags were introduced to address the previously reported accumulation of repressor proteins. In addition, D91 from the degradation tag mutant library was introduced into E. coli to synthesize ergothioneine using a temperature-tuned expression delay timer. The yield of 307 mg/L was obtained in 48 h under shake-flask fermentation and 7.5 g/L in a 2 L bioreactor after optimizing the fermentation conditions and S-adenosylmethionine supply. This study provides a new approach to long-term effective gene expression at lower cost, thus enriching the library of programmable expression elements.
A case-study evaluation of a pBR322-derived expression system, previously applied to therapeutic peptides and insulin analogs, in combination with fed-batch cultivation for recombinant production of methionine aminopeptidase in E. coli, evaluating the performance of this system for methionine aminopeptidase as a stress-sensitive model protein under the tested conditions without a side-by-side comparison with alternative expression systems.
G. Kuznetsov, Marina Yarovikova, E. Buslaeva et al.· Protein Expression and Purif...· 0 citations