Difference between revisions of "Part:BBa K1150004"

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Phytochrome B is a photoreceptor which detects red and far-red light. In <i> Arabidopsis thaliana </i>, Phytochrome B predominantly controls seedling establishment. It is a protein with a molecular mass of 125 kDa that is predominantly located in the cytoplasma. Its structure can be roughly divided in two parts: The N-terminal part, regulatory and photosensory, and the C-terminal part, regulatory. The N-terminal part is covalently bound to phytochromibilin. Phytochromibilin is a linear tetrapyrol that undergoes conformational changes upon radiation of either red- or far red-light when bound to the phytochrome moiety. This conformational change is responsible for the photosensory properties of PhyB. [1]<br>
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Phytochrome B is a photoreceptor which detects red and far-red light. In <i> Arabidopsis thaliana</i>, Phytochrome B predominantly controls seedling establishment. It is a protein with a molecular mass of 125 kDa that is predominantly located in the cytoplasm. Its structure can be roughly divided in two parts: The N-terminal regulatory and photosensory part and the C-terminal regulatory part. The N-terminal part is covalently bound to phytochromibilin. Phytochromibilin is a linear tetrapyrol that undergoes conformational changes upon radiation of either red- or far red-light when bound to the phytochrome moiety. This conformational change is responsible for the photosensory properties of PhyB. [1]<br>
 
Illumination with red light (660 nm wavelength) leads to binding of Phytochrome Interaction Factor 6 (PIF6). The interaction can be abolished by illumination with far-red light (740 nm) wavelength. <br>
 
Illumination with red light (660 nm wavelength) leads to binding of Phytochrome Interaction Factor 6 (PIF6). The interaction can be abolished by illumination with far-red light (740 nm) wavelength. <br>
Team Freiburg 2013 uses Phy B to induce gene activation or repression via light stimulus. Therefore Phy B can be fused to effector domains like VP16 or KRAB.
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Team Freiburg 2013 uses Phy B to induce gene activation or repression via light stimulus. Therefore Phy B can be fused to effector domains like [https://parts.igem.org/Part:BBa_K1150001 VP16] or [https://parts.igem.org/Part:BBa_K1150002 KRAB].
  
  

Revision as of 20:57, 4 October 2013

PhyB

PhyB
Function Photoreceptor
Use in Mammalian cells
RFC standard RFC 25
Backbone pSB1C3
Organism Arabidopsis thaliana
Source AG Weber, Freiburg
Submitted by [http://2013.igem.org/Team:Freiburg Freiburg 2013]

Phytochrome B is a photoreceptor which detects red and far-red light. In Arabidopsis thaliana, Phytochrome B predominantly controls seedling establishment. It is a protein with a molecular mass of 125 kDa that is predominantly located in the cytoplasm. Its structure can be roughly divided in two parts: The N-terminal regulatory and photosensory part and the C-terminal regulatory part. The N-terminal part is covalently bound to phytochromibilin. Phytochromibilin is a linear tetrapyrol that undergoes conformational changes upon radiation of either red- or far red-light when bound to the phytochrome moiety. This conformational change is responsible for the photosensory properties of PhyB. [1]
Illumination with red light (660 nm wavelength) leads to binding of Phytochrome Interaction Factor 6 (PIF6). The interaction can be abolished by illumination with far-red light (740 nm) wavelength.
Team Freiburg 2013 uses Phy B to induce gene activation or repression via light stimulus. Therefore Phy B can be fused to effector domains like VP16 or KRAB.



Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 490
    Illegal BamHI site found at 572
    Illegal XhoI site found at 523
    Illegal XhoI site found at 542
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal SapI site found at 739

References

[1] Lars-Oliver Essen, Jo Mailliet, and Jon Hughes 2008; Quail 2002