|
|
| (31 intermediate revisions not shown) |
| Line 1: |
Line 1: |
| - | {{:Team:EPF-Lausanne/Template/Header}} | + | {{:Team:EPF-Lausanne/Template/Header|project}} |
| | | | |
| | = Introduction = | | = Introduction = |
| | | | |
| - | == How LovTAP is thought to work ==
| |
| | | | |
| - | === Allosteric regulation ===
| |
| | | | |
| - | In a protein, generally an enzyme, an allosteric site is any part of the protein other than the active site.
| |
| | | | |
| - | 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,
| + | |
| - | a group of genes studied in E. coli that are required for the synthesis of the amino acid tryptophan.
| + | |
| - | The expression of these genes can be blocked by the homodimeric protein tryptophan repressor
| + | |
| - | (TrpR), by binding the operator of the operon. TrpR repressing function is only active when
| + | |
| - | tryptophan is bound to its allosteric sites, i.e. it blocks the production of tryptophan when the
| + | |
| - | concentration of tryptophan is high.
| + | |
| | | | |
| - | === LovTAP ===
| |
| | | | |
| - | 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
| |
| - | its activity can be controlled by light. This is done by fusing it to a light sensitive protein, the
| |
| - | plant phototropin LOV2 (Light-Oxygen-Voltage), whose sensitivity to blue light is conferred by the
| |
| - | ligand chromophore flavin mononucleotide (FMN). The fusion is done in a way that both domains
| |
| - | share a common α-helix, which would create a sort of lever that could transfer the conformational
| |
| - | changes in LOV2 when light-activated towards TrpR, triggering its activation.
| |
| | | | |
| | | | |
"
