Team:EPF-Lausanne/Modeling/LovTAP

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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.
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== How LovTAP is thought to work ==
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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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Latest revision as of 09:47, 26 September 2012

Introduction

How LovTAP is thought to work