ArticleScientific reports2018
Optimization of ClpXP activity and protein synthesis in an E. coli extract-based cell-free expression system.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Review
- Regulatory Components for Bacterial Cell-Free Systems Engineering.ACS synthetic biology · 2024Review
- Expanding luciferase reporter systems for cell-free protein expression.Scientific reports · 2022Article
- Synthetic cell-based materials extract positional information from morphogen gradients.Science advances · 2022Article
- Lipid sponge droplets as programmable synthetic organelles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Metabolic Profiling ofIndustrial & engineering chemistry research · 2019Article
- Cell-free microcompartmentalised transcription-translation for the prototyping of synthetic communication networks.Current opinion in biotechnology · 2019Review
- Proteolysis mediated by the membrane-integrated ATP-dependent protease FtsH has a unique nonlinear dependence on ATP hydrolysis rates.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
5 authors.
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Abstract
Protein degradation is a fundamental process in all living cells and is essential to remove both damaged proteins and intact proteins that are no longer needed by the cell. We are interested in creating synthetic genetic circuits that function in a cell-free expression system. This will require not only an efficient protein expression platform but also a robust protein degradation system in cell extract. Therefore, we purified and tested the activity of E. coli ClpXP protease in cell-free transcription-translation (TX-TL) systems that used E. coli S30 cell extract. Surprisingly, our studies showed that purified ClpXP added to the TX-TL system has very low proteolytic activity. The low activity of ClpXP was correlated with the rapid consumption of adenosine triphosphate (ATP) in cell extract. We improved the activity of ClpXP in cell extract by adding exogenous ATP and an energy regeneration system. We then established conditions for both protein synthesis, and protein degradation by ClpXP to occur simultaneously in the TX-TL systems. The optimized conditions for ClpXP activity will be useful for creating tunable synthetic genetic circuits and in vitro synthetic biology.
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