Protein_Domain
Gal4DB
Part:BBa_J176020:Design
Designed by: Karmella Haynes Group: Haynes Lab (2011-09-29)
Gal4 DB
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal XhoI site found at 218
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 137
Design Notes
- Gel-shift characterization: The the DNA-binding stoichiometry of the 1-147 N-terminal portion of Gal4 is Gal4DB:UAS 17-mer = 2:1. [1]. The 17-mer is 5'-CGGAAGACTCTCCTCCG.
- The Haynes lab UAS BioBrick 5xGal4: BBa_J176019 has 5 copies of a similar 17-mer, each connected by 2 bp (spacer): 5'-CGGAgtACTgTCCTCCG (ag)
Source
TBA
References
1. Carey, M., Kakidani, H., Leatherwood, J., Mostashari, F., & Ptashne, M. (1989). An amino-terminal fragment of GAL4 binds DNA as a dimer. Journal of Molecular Biology, 209(3), 423–432.