Part:BBa_K4138004
SOPP3-2ABH
Profile
Fusion construct made of the photosensitizer SOPP3 (BBa_K4138001) and the phosphate-binding protein 2ABH (BBa_K4138000). SOPP3 is engineered synthetically. Its protein structure is based on a protein originating in Arabidopsis thaliana and is light-sensitive. 2ABH is a phosphate-binding protein found in Escherichia coli. Both proteins, SOPP3 and 2ABH, are linked by a spacer (BBa_K4138007).
Base pairs SOPP3: 381 bp
Base pairs Spacer: 72 bp
Base pairs 2ABH: 963 bp
Usage and Biology
The phosphate-binding protein 2ABH binds phosphate with high affinity and allows the release of the bound phosphate in vitro only under extreme conditions. The fusion with the photosensitizer SOPP3 enables the release of the phosphate by light irradiation. For this purpose, the protein constructs were irradiated with blue light. Blue light induces the production of reactive oxygen species (ROS). The synthesized ROS lead to chemical degradation of 2ABH and thus cause the release of the phosphate bound to 2ABH. Upon irradiation, the chemical degradation follows in minutes [1], [2], [3].
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 187
Illegal PstI site found at 316
Illegal PstI site found at 346 - 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 187
Illegal PstI site found at 316
Illegal PstI site found at 346 - 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 187
Illegal PstI site found at 316
Illegal PstI site found at 346 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 187
Illegal PstI site found at 316
Illegal PstI site found at 346
Illegal AgeI site found at 1098 - 1000COMPATIBLE WITH RFC[1000]
Transformation and Expression
The protein fusion construct inserted in the pET-28a(+) vector was transformed into chemically competent E. coli cells via heat shock. After transformation, the SOPP3-2ABH construct was expressed in E. coli BL21(DE3) gold.
Medium used for
Transformation: LB-medium with the addition of kanamycin
Expression: TB-medium with the addition of kanamycin, IPTG-induced
References
[1] Torra, J., Lafaye, C., Signor, L. et al. Tailing miniSOG: structural bases of the complex photophysics of a flavin-binding singlet oxygen photosensitizing protein. Sci Rep 9, 2428 (2019). https://doi.org/10.1038/s41598-019-38955-3
[2] Christie JM, Salomon M, Nozue K, Wada M, Briggs WR. LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): binding sites for the chromophore flavin mononucleotide. Proc Natl Acad Sci U S A. (1999). https://doi.org/10.1073/pnas.96.15.8779
[3] Z. Wang, A. Choudhary, P.S. Ledvina, F.A. Quiocho, Fine tuning the specificity of the periplasmic phosphate transport receptor. Site-directed mutagenesis, ligand binding, and crystallographic studies., Journal of Biological Chemistry, Volume 269, Issue 40, 1994, Pages 25091-25094, https://doi.org/10.1016/S0021-9258(17)31503-X.
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