High energy-charged cell factory for heterologous protein synthesis
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- Catholic University of Korea, Biotechnology
- Catholic Univ. of Korea,
- Korea Advanced Institute of Science and Technology, Chemical and Biomolecular Engineering, and Bioinformatics Research Center
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- Document Type:
- Manuscript
- Date:
- Received 06 November 2009 01:43 UTC; Posted 06 November 2009
- Subjects:
- Biotechnology
- Abstract:
Overexpression of gluconeogenic phosphoenolpyruvate carboxykinase (PCK) under glycolytic conditions enables Escherichia coli to maintain a greater intracellular ATP concentration and, consequently, to up-regulate genes for amino acid and nucleotide biosynthesis. To investigate the effect of a high intracellular ATP concentration on heterologous protein synthesis, we studied the expression of a foreign gene product, enhanced green fluorescence protein (eGFP), under control of the T7 promoter in E. coli BL21(DE3) strain overexpressing PCK. This strain was able to maintain twice as much intracellular ATP and to express two times more foreign protein than the control strain. These results indicate that a high energy-charged cell can be beneficial as a protein-synthesizing cell factory. The potential uses of such a cell factory are discussed.
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- This document is licensed to the public under the Creative Commons Attribution 3.0 License
- How to cite this document:
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Kim, Pil, Kim, Hye Jung, Kwon, Yeong Deok, and Lee, Sang Yup. High energy-charged cell factory for heterologous protein synthesis. Available from Nature Precedings <http://hdl.handle.net/10101/npre.2009.3953.1> (2009)
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