Composite

Part:BBa_K1638011

Designed by: Jens Sivkr Pettersen   Group: iGEM15_SDU-Denmark   (2015-05-22)
Revision as of 09:23, 18 September 2015 by Jpettersen (Talk | contribs)

Leucine zipper fused to T18 domain of cyaA from Bordetella pertussis

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 [1]. 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 a cAMP-induced reporter system, one can detect correct complementation.

Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Unknown
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 711
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 252
    Illegal NgoMIV site found at 662
    Illegal AgeI site found at 468
  • 1000
    COMPATIBLE 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.


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