Difference between revisions of "Part:BBa K1638031"

Revision as of 09:04, 18 September 2015

Leucine zipper fused to T18 domain of cyaA with cAMP-induced RFP generator

This part consist of the leucine zipper region of the yeast GCN4 protein fused to the T18 domain as used in the bacterial two-hybrid system. This part allows test of functional complementation between the T18 and T25 domain. When T18-zip and T25-zip are co-transformed, the homodimerisation of the two leucine zipper will cause association of the T18 and T25 domain and catalyse formation of cAMP. By using the cAMP-induced reporter construct (mRFP generator controlled by the promoter PcstA), one can detect correct complementation by the appearance of red colonies.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
INCOMPATIBLE WITH RFC[21]
Illegal BamHI site found at 1719
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal NgoMIV site found at 1260
Illegal NgoMIV site found at 1670
Illegal AgeI site found at 712
Illegal AgeI site found at 824
Illegal AgeI site found at 1476
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K1638031 short</partinfo>
-This part consist of the leucine zipper region of the yeast GCN4 protein fused to the T18 domain as used in the bacterial two-hybrid system. This part allows test of functional complementation between the T18 and T25 domain. When T18-zip and T25-zip are co-transformed, the homodimerisation of the two leucine zipper will cause association of the T18 and T25 domain and catalyse formation of cAMP. By using the cAMP-induced reporter construct ([https://parts.igem.org/Part:BBa_K861173 RFP controlled by the promoter PstA]), one can detect correct complementation by the appearance of red colonies.
+This part consist of the leucine zipper region of the yeast GCN4 protein fused to the T18 domain as used in the bacterial two-hybrid system. This part allows test of functional complementation between the T18 and T25 domain. When T18-zip and T25-zip are co-transformed, the homodimerisation of the two leucine zipper will cause association of the T18 and T25 domain and catalyse formation of cAMP. By using the cAMP-induced reporter construct ([https://parts.igem.org/Part:BBa_K861173 mRFP generator controlled by the promoter PcstA]), one can detect correct complementation by the appearance of red colonies.
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