Difference between revisions of "Part:BBa K4375019"

 
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<partinfo>BBa_K4375019 short</partinfo>
 
<partinfo>BBa_K4375019 short</partinfo>
  
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This device is meant for the light-inducible production of Cytolysin A (BBa_K811000), a pore-forming toxin. To achieve this, we used a modified arabinose operator system, where the transcription factor, AraC, is engineered to homodimerise by blue-light instead of arabinose binding. Its called BLADE and described in BBa_K4375003, and it is produced under the strong constitutive promoter J23101*.
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This device is meant for the light-inducible production of Cytolysin A (BBa_K811000), a pore-forming toxin. To achieve this, we used a modified arabinose operator system, where the transcription factor, AraC, is engineered to homodimerise by blue-light instead of arabinose binding. It's called BLADE and described in BBa_K4375003, and it is produced under the strong constitutive promoter J23101*.
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==Usage and Biology==
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ClyA is a protein native to E. coli, Shigella flexneri, and Salmonella typhi that is capable of forming 13-mer pore complexes in a redox-independent manner. Expression of clyA in the absence of other hemolytic toxins is sufficient to induce hemolysis experimentally, and is therefore considered to be a potent cytolytic agent. ClyA is functional immediately following translation of mRNA to protein.
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===Usage and Biology===
 
  
 
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Revision as of 09:33, 7 October 2022


Blue light inducible production of Cytolysin A (BLADE)

This device is meant for the light-inducible production of Cytolysin A (BBa_K811000), a pore-forming toxin. To achieve this, we used a modified arabinose operator system, where the transcription factor, AraC, is engineered to homodimerise by blue-light instead of arabinose binding. It's called BLADE and described in BBa_K4375003, and it is produced under the strong constitutive promoter J23101*.


Usage and Biology

ClyA is a protein native to E. coli, Shigella flexneri, and Salmonella typhi that is capable of forming 13-mer pore complexes in a redox-independent manner. Expression of clyA in the absence of other hemolytic toxins is sufficient to induce hemolysis experimentally, and is therefore considered to be a potent cytolytic agent. ClyA is functional immediately following translation of mRNA to protein.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 7
    Illegal NheI site found at 29
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 1144
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 979
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal SapI site found at 961