Team:NTHU Formosa/Parts

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Parts&Component

TEV protease

HTML Table

Name	Type	Description
BBa_K2635000	BBa_K2635001	BBa_K2635002	BBa_K2635003	BBa_K2635004	BBa_K2635005	BBa_K2635006	BBa_K2635007	BBa_K2635008	BBa_K2635009	BBa_K2635010	BBa_K2635011	BBa_K2635012	BBa_K2635013
composite	composite	basic	basic	basic	basic	basic	basic	basic	basic	basic	basic	basic	basic
Ernst Handel	Roland Mendel	Austria
Island Trading	Helen Bennett	UK
Laughing Bacchus Winecellars	Yoshi Tannamuri	Canada
Magazzini Alimentari Riuniti	Giovanni Rovelli	Italy

1.What is bioluminescence?
Bioluminescence is found in living organism. It’s light produced by chemical reaction in which luciferase catalyzed substrates and result in the emission of light.

2.Bioluminescence vs. Fluorescence
Bioluminescence results from chemical reaction which convert chemical energy to light energy. About 20% of the converted energy is released in the form of heat. Fluorescence is radiation emission, usually visible light. It occurs when the excited orbital electrons fall back to ground state and release the energy as light and heat.

3.About luciferase:
Since 1986, the discoveries of bioluminescence, the firefly luciferase, Renilla luciferase and NanoLuc luciferase, are nonstop. The firefly Luciferase has been widely used as sensor target after successfully cloned. Alternate bioluminescent reporter systems like these are the most common bioluminescence assays, which induce bioluminescence by substrates. The bioluminescence we use in our project is the codon-optimized self-directed bacterial luciferase gene cassette (lux). Lux is very unique among the present bioluminescence systems due to its ability to retrieves intercellular components to synthesize all substrates needed for its production of light.

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TEV proteases are the 27kDa catalytic domains of the NIa (Nuclear Inclusion a) protein encoded by Tobacco Etch Virus (TEV), where TEV proteases cut polyproteins into single proteins during biogenesis. TEV proteases recognize a linear epitope of the general form E-Xaa-Xaa-Y-Xaa-Q-(G/S) and cut the linkage between Q and G/S (Xaa can be freely substituted because variability in these positions was found in the natural cleavage sites of TEV’s polyprotein). Comparison of cleavage efficiency of different substract sequences demonstrated that “ENLYFQS” is the most efficient substrate sequence. The high-specificity of TEV’s cleavage makes it a popular tool for direct expression in living cells and protein purification.