Difference between revisions of "Team:Manchester/Description"
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| + | <h1 style="font-size:20px"> Mechanism 2</h1> | ||
| + | <h1 style="font-size:40px; color:orange; text-shadow: 1px 1px yellow">Inducible Gene Switch</h1> | ||
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<p style="font-size: 20px;text-align:left">The <i>alc</i> gene expression system is one of the most reliable chemically inducible gene switches for use in plants and fungus. This system relies on the ability of AlcR, a transcription factor, to bind to its target <i>alcA</i> promoter (alcA<sup>P</sup>). Based on this, we have engineered <i>Escherichia coli</i> K-12 derivative DH5α and BL21 to induce expression of chromoproteins when AlcR binds to alcA<sup>P</sup> in the presence of ethanol <sup>[1]</sup>. | <p style="font-size: 20px;text-align:left">The <i>alc</i> gene expression system is one of the most reliable chemically inducible gene switches for use in plants and fungus. This system relies on the ability of AlcR, a transcription factor, to bind to its target <i>alcA</i> promoter (alcA<sup>P</sup>). Based on this, we have engineered <i>Escherichia coli</i> K-12 derivative DH5α and BL21 to induce expression of chromoproteins when AlcR binds to alcA<sup>P</sup> in the presence of ethanol <sup>[1]</sup>. | ||
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Revision as of 22:09, 26 September 2016
Project Overview
Mechanism 1
Cell Free Mechanism
Mechanism 2
Inducible Gene Switch
The alc gene expression system is one of the most reliable chemically inducible gene switches for use in plants and fungus. This system relies on the ability of AlcR, a transcription factor, to bind to its target alcA promoter (alcAP). Based on this, we have engineered Escherichia coli K-12 derivative DH5α and BL21 to induce expression of chromoproteins when AlcR binds to alcAP in the presence of ethanol [1].
Reference
- Panozzo, C., Capuano, V., Fillinger, S. and Felenbok, B. (1997) ‘The zinc binuclear cluster Activator AlcR is able to bind to single sites but requires multiple repeated sites for synergistic activation of the alcA gene in Aspergillus nidulans’, Journal of Biological Chemistry, 272(36), pp. 22859–22865.
