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- | {{:Team:EPF-Lausanne/Template/Header}} | + | {{:Team:EPF-Lausanne/Template/Header|project}} |
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| = Introduction = | | = Introduction = |
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- | == How LovTAP is thought to work ==
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- | === Allosteric regulation ===
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- | In a protein, generally an enzyme, an allosteric site is any part of the protein other than the active site.
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- | Allosteric regulation of a protein consists in modifying its properties by interacting with an allosteric site.
| + | == How LovTAP is thought to work == |
- | One example would be the regulation in the tryptophan (trp) operon,
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- | a group of genes studied in E. coli that are required for the synthesis of the amino acid tryptophan.
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- | The expression of these genes can be blocked by the homodimeric protein tryptophan repressor
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- | (TrpR), by binding the operator of the operon. TrpR repressing function is only active when
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- | tryptophan is bound to its allosteric sites, i.e. it blocks the production of tryptophan when the
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- | concentration of tryptophan is high.
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- | === LovTAP ===
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- | In a paper published in 2008 [http://www.pnas.org/content/105/31/10709.abstract], Strickland et al. propose to modify the protein TrpR such that
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- | its activity can be controlled by light. This is done by fusing it to a light sensitive protein, the
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- | plant phototropin LOV2 (Light-Oxygen-Voltage), whose sensitivity to blue light is conferred by the
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- | ligand chromophore flavin mononucleotide (FMN). The fusion is done in a way that both domains
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- | share a common α-helix, which would create a sort of lever that could transfer the conformational
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- | changes in LOV2 when light-activated towards TrpR, triggering its activation.
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- | ==== VP16 ===
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- | [http://pubs.acs.org/doi/full/10.1021/bi0482912|Paper] stating that the part of VP16 we used (456-490) behaves as transcriptional activator.
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| {{:Team:EPF-Lausanne/Template/Footer}} | | {{:Team:EPF-Lausanne/Template/Footer}} |