Team:HKU-Hong Kong/Parts

From 2011.igem.org

(Difference between revisions)

Latest revision as of 17:30, 5 October 2011

Sample Data Page

By expressing the tetR-HNS fusion proteins, the tetR part of the proteins wound recognize and specifically bind to the 2 tetR binding region (tetO2).Thus in our designed operator- repressor binding, the presence of 2 tetR binding sites are used to enhance the binding of tetR part of the fusion proteins. As the fusion proteins bound to tetO, it is expected that the H-NS part of the fusion protein would attract and oligomerize with other native H-NS proteins inside the cell. With the oligomerization of the fusion proteins and native H-NS, the DNA covered by the oligomers is expected to trap the RNA polymerase during transcription, thus gene (GFP) repression is achieved.

Experience:

We have entered the confirmation data for the characterization of the selected constitutive promoters we have used. Of the 4 promoters we have used in the project, our team considered that J23109 or J23116 are more suitable promoters in creating the super silencer repression system.

These parts are:

[http://partsregistry.org/Part:BBa_J23103:Experience BBa_J23103 ]

[http://partsregistry.org/Part:BBa_J23106:Experience BBa_J23106 ]

[http://partsregistry.org/Part:BBa_J23109:ExperienceBBa_J23109 ]

[http://partsregistry.org/Part:BBa_J23116:ExperienceBBa_J23116 ]

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 |style="font-family: georgia, helvetica, arial, sans-serif;font-size:2em;color:#01DF01;"|Sample Data Page
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 <div ALIGN=CENTER>
   {| style="width:254px;background:#99EE63;text-align:center;font-family: georgia, helvetica, arial, sans-serif;color:#000000;margin- top:5px;padding: 2px;" cellspacing="5";
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-By expressing the tetR:H-NS fusion proteins, the tetR part of the proteins wound recognize and specifically bind to the tetR binding region (tetO2). There are two tet-R binding sites as tet-R form a dimer as in the tet repressor- operator system. As the fusion proteins bound to tet-O, it is expected that the H-NS part of the fusion protein would attract and oligomerize with other native H-NS proteins inside the cell.  With the oligomerization of the fusion proteins and native H-NS, the DNA covered by the oligomers is expected to trap the RNA polymerase during transcription, thus gene (GFP) repression is achieved.
+By expressing the tetR-HNS fusion proteins, the tetR part of the proteins wound recognize and specifically bind to the 2 tetR binding region (tetO2).Thus in our designed operator- repressor binding, the presence of 2 tetR binding sites are used to enhance the binding of tetR part of the fusion proteins. As the fusion proteins bound to tetO, it is expected that the H-NS part of the fusion protein would attract and oligomerize with other native H-NS proteins inside the cell. With the oligomerization of the fusion proteins and native H-NS, the DNA covered by the oligomers is expected to trap the RNA polymerase during transcription, thus gene (GFP) repression is achieved.
+|-
+|style="width:900px;"|
+<div ALIGN=CENTER>
+ {| style="width:254px;background:#99EE63;text-align:center;font-family: georgia, helvetica, arial, sans-serif;color:#000000;margin- top:5px;padding: 2px;" cellspacing="5";
+ |-
+ |[[Image:Sample Data Table.png|650px]]
+ |-
+ |}
+</div>
+|}
+{| style="width:900px;background:#000000;text-align:justify;font-family: georgia, helvetica, arial, sans-serif;color:#ffffff;margin-top:25px;" cellspacing="20"
+|-
+|style="width:900px;"|
+'''Experience:'''
+We have entered the confirmation data for the characterization of the selected constitutive promoters we have used. Of the 4 promoters we have used in the project, our team considered that J23109 or J23116 are more suitable promoters in creating the super silencer repression system.
-'''Parts that we have created:'''
+These parts are:
-(The favorite parts are selected based on the potential to be used in our Super silencer repression system)
 {| style="width:900px;background:#000000;text-align:justify;font-family: georgia, helvetica, arial, sans-serif;color:#ffffff;margin-top:25px;" cellspacing="20"
 |-
-|style="font-family: georgia, helvetica, arial, sans-serif;font-size:2em;color:#01DF01;" align="left"|[http://partsregistry.org/Part:BBa_K544001 '''BBa_K544001''' ]
+|style="font-family: georgia, helvetica, arial, sans-serif;font-size:1.5em;color:#01DF01;" align="left"|[http://partsregistry.org/Part:BBa_J23103:Experience '''BBa_J23103''' ]
-|style="font-family: georgia, helvetica, arial, sans-serif;font-size:2em;color:#01DF01;" align="centre"|[http://partsregistry.org/BBa_K544002 '''BBa_K544002''' ]
+|style="font-family: georgia, helvetica, arial, sans-serif;font-size:1.5em;color:#01DF01;" align="centre"|[http://partsregistry.org/Part:BBa_J23106:Experience '''BBa_J23106''' ]
-|style="font-family: georgia, helvetica, arial, sans-serif;font-size:2em;color:#01DF01;" align="right"|[http://partsregistry.org/BBa_K544003'''BBa_K544003''' ]
+|style="font-family: georgia, helvetica, arial, sans-serif;font-size:1.5em;color:#01DF01;" align="right"|[http://partsregistry.org/Part:BBa_J23109:Experience'''BBa_J23109''' ]
-|-
+|style="font-family: georgia, helvetica, arial, sans-serif;font-size:1.5em;color:#01DF01;" align="right"|[http://partsregistry.org/Part:BBa_J23116:Experience'''BBa_J23116''' ]
-|style="font-family: georgia, helvetica, arial, sans-serif;font-size:2em;color:#01DF01;" align="left"|[http://partsregistry.org/BBa_K544012'''BBa_K544012''' ]
-|style="font-family: georgia, helvetica, arial, sans-serif;font-size:2em;color:#01DF01;" align="centre"|[http://partsregistry.org/BBa_K544011 '''BBa_K544011''' ]
-|style="font-family: georgia, helvetica, arial, sans-serif;font-size:2em;color:#01DF01;" align="right"|[http://partsregistry.org/BBa_K544013 '''BBa_K544013''' ]
-|-
-|style="font-family: georgia, helvetica, arial, sans-serif;font-size:2em;color:#01DF01;" align="left"|[http://partsregistry.org/BBa_K544014 '''BBa_K544014''' ]
-|style="font-family: georgia, helvetica, arial, sans-serif;font-size:2em;color:#01DF01;" align="centre"|[http://partsregistry.org/BBa_K544015 '''BBa_K544021''' ]
 |-
+|}