Difference between revisions of "Part:BBa K1592006"
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<partinfo>BBa_K1592006 short</partinfo> | <partinfo>BBa_K1592006 short</partinfo> | ||
− | CIB1, a basic helix-loop-helix (bHLH) protein, would interact with cryptochrome 2 (CRY2), a blue light stimulated photoreceptor, when exposed to blue light. The CRY2/CIB1 interaction is entirely genetically encoded and does not require addition of any exogenous cofactors. These modules require no exogenous chromophore, are reversible within minutes, trigger protein translocation on a sub-second time scale, and even allow potential use in vivo in whole organisms. | + | CIB1, a basic helix-loop-helix (bHLH) protein, would interact with cryptochrome 2 (CRY2), a blue light stimulated photoreceptor, when exposed to blue light. |
+ | The CRY2/CIB1 interaction is entirely genetically encoded and does not require addition of any exogenous cofactors. These modules require no exogenous chromophore, are reversible within minutes, trigger protein translocation on a sub-second time scale, and even allow potential use in vivo in whole organisms. | ||
This fusion protein is for use in a yeast-two-hybrid system, and a Gal4 DNA activating domain fused to its C terminus. | This fusion protein is for use in a yeast-two-hybrid system, and a Gal4 DNA activating domain fused to its C terminus. | ||
To regulate DNA transcription by blue light, the system is based on a two-hybrid interaction in which a light-mediated protein interaction brings together two halves (a binding domain and an activation domain) of a split transcription factor. If we remove the stimulation of blue light, dark reversion of CRY2 will dissociate the interaction with CIB1 and halt Gal4-dependent transcription. | To regulate DNA transcription by blue light, the system is based on a two-hybrid interaction in which a light-mediated protein interaction brings together two halves (a binding domain and an activation domain) of a split transcription factor. If we remove the stimulation of blue light, dark reversion of CRY2 will dissociate the interaction with CIB1 and halt Gal4-dependent transcription. |
Revision as of 09:33, 4 September 2015
GalAD-CIB1 Fusion for Yeast-Two-Hybrid
CIB1, a basic helix-loop-helix (bHLH) protein, would interact with cryptochrome 2 (CRY2), a blue light stimulated photoreceptor, when exposed to blue light. The CRY2/CIB1 interaction is entirely genetically encoded and does not require addition of any exogenous cofactors. These modules require no exogenous chromophore, are reversible within minutes, trigger protein translocation on a sub-second time scale, and even allow potential use in vivo in whole organisms. This fusion protein is for use in a yeast-two-hybrid system, and a Gal4 DNA activating domain fused to its C terminus. To regulate DNA transcription by blue light, the system is based on a two-hybrid interaction in which a light-mediated protein interaction brings together two halves (a binding domain and an activation domain) of a split transcription factor. If we remove the stimulation of blue light, dark reversion of CRY2 will dissociate the interaction with CIB1 and halt Gal4-dependent transcription.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 445
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 407
Illegal XhoI site found at 1474 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 568
Illegal AgeI site found at 1461 - 1000COMPATIBLE WITH RFC[1000]