Difference between revisions of "Part:BBa K1638030"
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<partinfo>BBa_K1638030 short</partinfo> | <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 mRFP generator controlled by the promoter PcstA]), 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 [1]. |
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<partinfo>BBa_K1638030 SequenceAndFeatures</partinfo> | <partinfo>BBa_K1638030 SequenceAndFeatures</partinfo> | ||
| − | + | ===References=== | |
| + | [1]: Karimova G, Pidoux J, Ullmann A, Ladant D. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proceedings of the National Academy of Sciences of the United States of America. 1998;95(10):5752-6. | ||
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===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K1638030 parameters</partinfo> | <partinfo>BBa_K1638030 parameters</partinfo> | ||
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Revision as of 09:23, 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 [1].
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 1851
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 712
Illegal AgeI site found at 824 - 1000COMPATIBLE WITH RFC[1000]
References
[1]: Karimova G, Pidoux J, Ullmann A, Ladant D. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proceedings of the National Academy of Sciences of the United States of America. 1998;95(10):5752-6.