Difference between revisions of "Part:BBa K4044008"
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<partinfo>BBa_K4044008 short</partinfo> | <partinfo>BBa_K4044008 short</partinfo> | ||
− | + | The BphP1 monomer competes for binding to the QPAS 1 domain, which leads to the rupture of the Gal4-QPAS 1 dimer and its dissociation from DNA. Under the influence of red light with a wavelength of 640 nm, active BphP1 passes into an inactivated dimerized state. In this case, Gal4-QPAS 1 reverts to the dimer state, binds to DNA and suppresses transcription of the reporter gene. | |
+ | Bacterio phyto chromium Bp hP 1 in the inactive state is an intact dimer. Bp hP 1 changes from an inactive dimerized state (Pr) to an active monomeric state (Zac) under the influence of radiation at 760 nm, which opens the binding site for its contacting compound Q-PAS1. The Gal4 transcription factor is attached to it via a peptide bond. Gal4-QPAS1 dimer bounds to DNA via two sites of trinucleotides in the promoter region for each Gal4 HTH domain, inhibiting transcription of the reporter gene. Under the influence of far red light with a wavelength of 760 nm, the expression of target genes is activated | ||
+ | There are several states of the ontogenetic system. Under the influence of far red light, BphP1 part of the chimeric protein BphP1 becomes active and binds to QPAS1-Gal4. This leads to the expression of target gene. Under the influence of red light, BphP1 is inactivated, QPAS1-Gal4 remains in the dimerized state. This leads to inhibition of transcription. | ||
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Revision as of 01:48, 22 October 2021
BphP1_QPAS1-Gal4 optogenetic system
The BphP1 monomer competes for binding to the QPAS 1 domain, which leads to the rupture of the Gal4-QPAS 1 dimer and its dissociation from DNA. Under the influence of red light with a wavelength of 640 nm, active BphP1 passes into an inactivated dimerized state. In this case, Gal4-QPAS 1 reverts to the dimer state, binds to DNA and suppresses transcription of the reporter gene. Bacterio phyto chromium Bp hP 1 in the inactive state is an intact dimer. Bp hP 1 changes from an inactive dimerized state (Pr) to an active monomeric state (Zac) under the influence of radiation at 760 nm, which opens the binding site for its contacting compound Q-PAS1. The Gal4 transcription factor is attached to it via a peptide bond. Gal4-QPAS1 dimer bounds to DNA via two sites of trinucleotides in the promoter region for each Gal4 HTH domain, inhibiting transcription of the reporter gene. Under the influence of far red light with a wavelength of 760 nm, the expression of target genes is activated There are several states of the ontogenetic system. Under the influence of far red light, BphP1 part of the chimeric protein BphP1 becomes active and binds to QPAS1-Gal4. This leads to the expression of target gene. Under the influence of red light, BphP1 is inactivated, QPAS1-Gal4 remains in the dimerized state. This leads to inhibition of transcription.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 815
Illegal PstI site found at 1112
Illegal PstI site found at 1559 - 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 7
Illegal NheI site found at 30
Illegal PstI site found at 815
Illegal PstI site found at 1112
Illegal PstI site found at 1559 - 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 301
Illegal BamHI site found at 1876
Illegal BamHI site found at 2969 - 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 815
Illegal PstI site found at 1112
Illegal PstI site found at 1559 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 815
Illegal PstI site found at 1112
Illegal PstI site found at 1559
Illegal NgoMIV site found at 457
Illegal NgoMIV site found at 1208
Illegal NgoMIV site found at 1705 - 1000COMPATIBLE WITH RFC[1000]