Difference between revisions of "Part:BBa K1638030"

Revision as of 09:05, 18 September 2015

Leucine zipper fused to T25 domain of cyaA with cAMP-induced RFP generator

This part consist of the leucine zipper region of the yeast GCN4 protein fused to the T25 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 1851
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal AgeI site found at 712
Illegal AgeI site found at 824
1000
COMPATIBLE WITH RFC[1000]

@@ Line 2: / Line 2: @@
 <partinfo>BBa_K1638030 short</partinfo>
-This part consist of the leucine zipper region of the yeast GCN4 protein fused to the T25 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 T25 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.
 <!-- Add more about the biology of this part here