Template:Team:Bonn:NetworkData
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content.titleShort = "Heat"; | content.titleShort = "Heat"; | ||
content.titleLong = "Using heat as a means of induction"; | content.titleLong = "Using heat as a means of induction"; | ||
- | content.summary= "Discussion of heat and it's advantages | + | content.summary= "Discussion of heat and it's advantages and disadvantages as an induction tool"; |
- | content.text= "Heat can be used to induce the expression of desired genes. This can be achieved via the linkage of heat-inducable promoters and the genomic sequence of the desired protein. These heat-inducable promoters are most commonly derived from the genes of heat-shock-proteins, whose cellular levels of concentrations are at least in part regulated via heat [33.1].</br></br>The main advantage for the use of heat lies in its simplicity, compared to other methods of induction. There is no need to modify the amino acid sequence of the targeted protein. Furthermore, the method of induction is rather simple, as it only requires the heat shock of the organism. However, therein also lies the biggest disadvantage of this method, as heat-shocking an organism triggers many, oftentimes undesired physiological reactions besides the expression of the desired gene [33.2][33.3]. Another disadvantage is that the usage of heat only offers induction of protein levels, and can not be used to modulate protein activity besides unspecific denaturation. Also, the spatiotemporal resolution of heat is rather low [33.2][33.3].</br><div class='content-image'><img src='https://static.igem.org/mediawiki/2013/d/df/Bonn-Heat-1.PNG'> </br>Diagram showing the activity of a heat-induced promoter in relation to the temperature of the applied heat-shock [33.3]</div></br>Furthermore, heat-induced promoters have a base level of activity, so through its usage only the effects of high level of protein on the organism can be examined [33.3] <h3>References</h3><a href='http://www.ncbi.nlm.nih.gov/pubmed/23912482'>[33.1] Zhang L. et al, Characterization of four heat-shock protein genes from Nile tilapia (Oreochromis niloticus) and demonstration of the inducible transcriptional activity of Hsp70 promoter. Fish Physiol Biochem. 2013 Aug 4</a></br> <a href='http://www.ncbi.nlm.nih.gov/pubmed/6322174'>[33.2] Bardwell JC, Craig EA. Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous. Proc Natl Acad Sci U S A. 1984 Feb;81(3):848-52</a></br><a href='http://www.ncbi.nlm.nih.gov/pubmed/10739675'>[33.3] Attila Ádám et al, Heat-Inducible Expression of a Reporter Gene Detected by Transient Assay in Zebrafish, Experimental Cell Research 256: 282-290 (2000)</a>"; | + | content.text= "Heat can be used to induce the expression of desired genes. This can be achieved via the linkage of heat-inducable promoters and the genomic sequence of the desired protein. These heat-inducable promoters are most commonly derived from the genes of heat-shock-proteins, whose cellular levels of concentrations are at least in part regulated via heat [33.1].</br></br>The main advantage for the use of heat lies in its simplicity, compared to other methods of induction. There is no need to modify the amino acid sequence of the targeted protein. Furthermore, the method of induction is rather simple, as it only requires the heat shock of the organism. However, therein also lies the biggest disadvantage of this method, as heat-shocking an organism triggers many, oftentimes undesired physiological reactions besides the expression of the desired gene [33.2][33.3]. Another disadvantage is that the usage of heat only offers induction of protein levels, and can not be used to modulate protein activity besides unspecific denaturation. Also, the spatiotemporal resolution of heat is rather low [33.2][33.3].</br><div class='content-image'><img src='https://static.igem.org/mediawiki/2013/d/df/Bonn-Heat-1.PNG'> </br>Diagram showing the activity of a heat-induced promoter in relation to the temperature of the applied heat-shock [33.3]</div></br>Furthermore, heat-induced promoters have a base level of activity, so through its usage only the effects of high level of protein on the organism can be examined [33.3] <h3>References</h3><a href='http://www.ncbi.nlm.nih.gov/pubmed/23912482'>[33.1] Zhang L. et al., 'Characterization of four heat-shock protein genes from Nile tilapia (Oreochromis niloticus) and demonstration of the inducible transcriptional activity of Hsp70 promoter.' Fish Physiol Biochem. 2013 Aug 4</a></br> <a href='http://www.ncbi.nlm.nih.gov/pubmed/6322174'>[33.2] Bardwell JC, Craig EA. 'Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous.' Proc Natl Acad Sci U S A. 1984 Feb;81(3):848-52</a></br><a href='http://www.ncbi.nlm.nih.gov/pubmed/10739675'>[33.3] Attila Ádám et al., 'Heat-Inducible Expression of a Reporter Gene Detected by Transient Assay in Zebrafish', Experimental Cell Research 256: 282-290 (2000)</a>"; |
content.type="Background"; | content.type="Background"; | ||
break; | break; |
Revision as of 19:35, 1 October 2013