ArticleACS chemical biology2014
Heat-shock response transcriptional program enables high-yield and high-quality recombinant protein production in Escherichia coli.
Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
- A biosensor toolbox for monitoring recombinant protein production inFrontiers in bioengineering and biotechnology · 2026Article
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- Constitutive Activation of RpoH and the Addition of L-arabinose Influence Antibiotic Sensitivity of PHL628Antibiotics (Basel, Switzerland) · 2024Article
- N-terminal Domain of TDP43 Enhances Liquid-Liquid Phase Separation of Globular Proteins.Journal of molecular biology · 2021Article
- Heat-responsive and time-resolved transcriptome and metabolome analyses of Escherichia coli uncover thermo-tolerant mechanisms.Scientific reports · 2020Article
- The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants.Nature communications · 2019Article
- Burden-driven feedback control of gene expression.Nature methods · 2018Article
- Translation efficiency is maintained at elevated temperature inThe Journal of biological chemistry · 2018Article
- Bacterial proteostasis balances energy and chaperone utilization efficiently.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Transcriptome analysis of Corynebacterium glutamicum in the process of recombinant protein expression in bioreactors.PloS one · 2017Article
- Fluorescence Turn-On Folding Sensor To Monitor Proteome Stress in Live Cells.Journal of the American Chemical Society · 2015Article
- Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.Cell reports · 2015Article
- Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The biosynthesis of soluble, properly folded recombinant proteins in large quantities from Escherichia coli is desirable for academic research and industrial protein production. The basal E. coli protein homeostasis (proteostasis) network capacity is often insufficient to efficiently fold overexpressed proteins. Herein we demonstrate that a transcriptionally reprogrammed E. coli proteostasis network is generally superior for producing soluble, folded, and functional recombinant proteins. Reprogramming is accomplished by overexpressing a negative feedback deficient heat-shock response transcription factor before and during overexpression of the protein-of-interest. The advantage of transcriptional reprogramming versus simply overexpressing select proteostasis network components (e.g., chaperones and co-chaperones, which has been explored previously) is that a large number of proteostasis network components are upregulated at their evolved stoichiometry, thus maintaining the system capabilities of the proteostasis network that are currently incompletely understood. Transcriptional proteostasis network reprogramming mediated by stress-responsive signaling in the absence of stress should also be useful for protein production in other cells.
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Registered trials
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