ArticleBiotechnology and bioengineering2014
Dynamic transcriptional response of Escherichia coli to inclusion body formation.
Article in Biotechnology and bioengineering, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Recombinant expression of insoluble enzymes in Escherichia coli: a systematic review of experimental design and its manufacturing implications.Microbial cell factories · 2021Pooled it
- Recombinant expression of natural Arabidopsis PRLIP1 variants reveals temperature-dependent differences in fluorescence and functional protein recovery in Escherichia coli.World journal of microbiology & biotechnology · 2026Article
- Dynamic feedback regulation for efficient membrane protein production using a small RNA-based genetic circuit in Escherichia coli.Microbial cell factories · 2022Article
- Directed Evolution of Soluble α-1,2-Fucosyltransferase Using Kanamycin Resistance Protein as a Phenotypic Reporter for Efficient Production of 2'-Fucosyllactose.Journal of microbiology and biotechnology · 2022Article
- Introducing a new anti-Veterinary research forum : an international quarterly journal · 2021Article
- Impact of the Expression System on Recombinant Protein Production inFrontiers in microbiology · 2021Article
- Production of Lysostaphin by Nonproprietary Method Utilizing a Promoter from Toxin-Antitoxin System.Molecular biotechnology · 2019Article
- Recombinant production of ESAT-6 antigen in thermoinducible Escherichia coli: the role of culture scale and temperature on metabolic response, expression of chaperones, and architecture of inclusion bodies.Cell stress & chaperones · 2019Article
- Selection of High Producers From Combinatorial Libraries for the Production of Recombinant Proteins inFrontiers in bioengineering and biotechnology · 2019Article
- Protein aggregates encode epigenetic memory of stressful encounters in individual Escherichia coli cells.PLoS biology · 2018Article
- Global proteome response ofEngineering in life sciences · 2017Article
- Awakening sleeping beauty: production of propionic acid in Escherichia coli through the sbm operon requires the activity of a methylmalonyl-CoA epimerase.Microbial cell factories · 2017Article
- Optimizing the expression of a Heterologous chitinase: A study of different promoters.Bioengineered · 2017Article
- Tunable recombinant protein expression in E. coli: promoter systems and genetic constraints.Applied microbiology and biotechnology · 2017Review
- Tunable recombinant protein expression in E. coli: enabler for continuous processing?Applied microbiology and biotechnology · 2016Review
- Article
- Genome engineering for improved recombinant protein expression in Escherichia coli.Microbial cell factories · 2014Review
- Soluble expression of pullulanase from Bacillus acidopullulyticus in Escherichia coli by tightly controlling basal expression.Journal of industrial microbiology & biotechnology · 2014Article
- ccSOL omics: a webserver for solubility prediction of endogenous and heterologous expression in Escherichia coli.Bioinformatics (Oxford, England) · 2014Article
- Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coli.Microbial cell factories · 2014Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Escherichia coli is used intensively for recombinant protein production, but one key challenge with recombinant E. coli is the tendency of recombinant proteins to misfold and aggregate into insoluble inclusion bodies (IBs). IBs contain high concentrations of inactive recombinant protein that require recovery steps to salvage a functional recombinant protein. Currently, no universally effective method exists to prevent IB formation in recombinant E. coli. In this study, DNA microarrays were used to compare the E. coli gene expression response dynamics to soluble and insoluble recombinant protein production. As expected and previously reported, the classical heat-shock genes had increased expression due to IB formation, including protein folding chaperones and proteases. Gene expression levels for protein synthesis-related and energy-synthesis pathways were also increased. Many transmembrane transporter and corresponding catabolic pathways genes had decreased expression for substrates not present in the culture medium. Additionally, putative genes represented over one-third of the genes identified to have significant expression changes due to IB formation, indicating many important cellular responses to IB formation still need to be characterized. Interestingly, cells grown in 3% ethanol had significantly reduced gene expression responses due to IB formation. Taken together, these results indicate that IB formation is complex, stimulates the heat-shock response, increases protein and energy synthesis needs, and streamlines transport and catabolic processes, while ethanol diminished all of these responses.
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