Difference between revisions of "Part:BBa M50095:Design"
 
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<partinfo>BBa_M50095 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_M50095 SequenceAndFeatures</partinfo>
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VP16 or trans-activating tegument protein 16, is a viral protein sourced from human herpes simplex virus. VP16 promotes a number of human transcription factors and acts as an activator to drive downstream gene transcription.
 
  
 
===Design Notes===
 
===Design Notes===
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Human herpes simplex virus
 
Human herpes simplex virus
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Supplemental Figures 2. "An optogenetic gene expression system with rapid activation and deactivation kinetics" Gardner et. al 2014, Nature Chemical Biology
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Supplemental Figures 2. "An optogenetic gene expression system with rapid activation and deactivation kinetics" Motta-Mena et. al 2014, Nature Chemical Biology
  
 
===References===
 
===References===
  
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"An optogenetic gene expression system with rapid activation and deactivation kinetics" Gardner et. al 2014, Nature Chemical Biology
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"An optogenetic gene expression system with rapid activation and deactivation kinetics" Motta-Mena et. al 2014, Nature Chemical Biology

Latest revision as of 01:23, 14 December 2017


VP16 - Herpes simplex virus transactivating protein


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]

Design Notes

This VP-16 was attached to a LOV-HTH optogenetic DNA binding domain, such that when the protein complex was exposed to light, and thus is able to bind DNA, the VP-16 can recruit transcription factors to the DNA and drive transcription. No changes were made to this sequence as it is already optimized for HEK293T cells.


Source

Human herpes simplex virus

Supplemental Figures 2. "An optogenetic gene expression system with rapid activation and deactivation kinetics" Motta-Mena et. al 2014, Nature Chemical Biology

References

"An optogenetic gene expression system with rapid activation and deactivation kinetics" Motta-Mena et. al 2014, Nature Chemical Biology