Team:Chiba/Project/oxidation

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Revision as of 03:51, 26 September 2013

iGEM-2013 Chiba

oxidation

Background

    Two proteins called glutathione and thioredoxin which have disulfide bond (-s-s-) in oxidized states exist in E.coli(WT). They play a role of redox control in E.coli.
    Oxidative stress avtivates glutathione reductase (gor) and thioredoxin reductase (trxB). Therefore, E.coli is constantly reductive.
    On the other hand, cytosol of yeast is oxidative originally and they can have magnetism, and be attracted by magnets.
    So, we thought changing the E.coli cytosol to oxidative state like yeast leads to be attracted by magnets.
    That's why knocking out trxB and gor is neccesary to acchive magnetism.

@@ Line 23: / Line 23: @@
 <p>
-	&nbsp;&nbsp;&nbsp;&nbsp;<i>E.coli</i> (wild type) can’t form the disulfide bonds because it has reductive state in cytosol.
+	&nbsp;&nbsp;&nbsp;&nbsp;Two proteins called glutathione and thioredoxin which have disulfide bond (-s-s-) in oxidized states exist in E.coli(WT). They play a role of redox control in E.coli.
-<br>&nbsp;&nbsp;&nbsp;&nbsp;We use the shuffle cell whose genes, <i>trxB</i> and <i>gor</i> are knocked out. <i>TrxB</i> and <i>gor</i> codes reductase which …  So shuffle cells have oxidative state enough to form the disulfide bonds.
+<br>&nbsp;&nbsp;&nbsp;&nbsp;Oxidative stress avtivates glutathione reductase (gor) and thioredoxin reductase (trxB). Therefore, E.coli is constantly reductive.<br>
+&nbsp;&nbsp;&nbsp;&nbsp;On the other hand, cytosol of yeast is oxidative originally and they can have magnetism, and be attracted by magnets.<br>
+&nbsp;&nbsp;&nbsp;&nbsp;So, we thought changing the E.coli cytosol to oxidative state like yeast leads to be attracted by magnets.<br>
+&nbsp;&nbsp;&nbsp;&nbsp;That's why knocking out trxB and gor is neccesary to acchive magnetism.
 </p>