Part:BBa_K1462510:Design
GAL1+YFP+SH3-lig+ADH1
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 150
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
This is the composite part, consist of the GAL1 promoter, YFP fusing with the SH3 ligand and the ADH1 terminator. Now we made this device to check whether the ligand owns the binding funtion or not. It helped us to affirm the scaffold protein and it's ligands can work.Besides, it's induced by the existence of galactose.
Source
We got the SH3 ligand from PCR. The YFP[BBa_E0030] was from the plate sent from the IGEM.Also the GAL1[BBa_J63006] and ADH1[BBa_J63002] were the same source from the plate.
References
[1] John E Dueber, Gabriel C Wu, G Reza Malmirchegini, et al.Synthetic protein scaffolds provide modular control
over metabolic flux.Nat Biotechnol. 2009 Aug;27(8):753-9.
[2] Schultz, J. et al. Specific interactions between the syntrophin PDZ domain and
voltage-gated sodium channels. Nat Struct Biol 5, 19-24 (1998).
[3] Kim, A.S., Kakalis, L.T., Abdul-Manan, N., Liu, G.A. & Rosen, M.K.
Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome
protein. Nature 404, 151-158 (2000).
[4] Wu, X. et al. Structural basis for the specific interaction of lysine-containing
proline-rich peptides with the N-terminal SH3 domain of c-Crk. Structure 3, 215-226 (1995).
[5] Harris, B.Z., Hillier, B.J. & Lim, W.A. Energetic determinants of internal motif
recognition by PDZ domains. Biochemistry 40, 5921-5930 (2001).
[6] Dueber, J.E., Yeh, B.J., Chak, K. & Lim, W.A. Reprogramming control of an
allosteric signaling switch through modular recombination. Science 301, 1904-1908 (2003).
[7] Nguyen, J.T., Turck, C.W., Cohen, F.E., Zuckermann, R.N. & Lim, W.A.
Exploiting the basis of proline recognition by SH3 and WW domains: design of
N-substituted inhibitors. Science 282, 2088-2092 (1998).