Difference between revisions of "Part:BBa K2923015"

 
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This composite part corresponds to the fusion protein between WT LexA repressor and PP7 coat protein. iGEM Strasbourg 2019 uses this protein as a part of constructed LexA based bacterial three-hybrid. LexA with wild type DNA binding domain fused to the PP7 coat protein and LexA with the mutated version of DNA binding domain fused to the MS2 coat protein. Respectively, these two hybrid proteins specifically recognize the mutated LexA operator sequence, which contains a wild-type half-site (CTGT) and a mutated operator half-site (CTGT) described by Dimitrova et al 1998 study. This construct allows recognition of MS2-MS2-Aptazyme-PP7-PP7.
 
This composite part corresponds to the fusion protein between WT LexA repressor and PP7 coat protein. iGEM Strasbourg 2019 uses this protein as a part of constructed LexA based bacterial three-hybrid. LexA with wild type DNA binding domain fused to the PP7 coat protein and LexA with the mutated version of DNA binding domain fused to the MS2 coat protein. Respectively, these two hybrid proteins specifically recognize the mutated LexA operator sequence, which contains a wild-type half-site (CTGT) and a mutated operator half-site (CTGT) described by Dimitrova et al 1998 study. This construct allows recognition of MS2-MS2-Aptazyme-PP7-PP7.
  
[[Image: MS2-LexA et PP7-LexA.jpg|700px|thumb|center| Figure: Schematic graphic of complete Aptazyme-induced bacterial three-hybrid system based on LexA heterodimer repressor]
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[[Image: MS2-LexA et PP7-LexA.jpg|700px|thumb|center| Figure: Schematic graphic of complete Aptazyme-induced bacterial three-hybrid system based on LexA heterodimer repressor
 
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Latest revision as of 10:11, 14 October 2019


PP7cp-LexA WT

This composite part corresponds to the fusion protein between WT LexA repressor and PP7 coat protein. iGEM Strasbourg 2019 uses this protein as a part of constructed LexA based bacterial three-hybrid. LexA with wild type DNA binding domain fused to the PP7 coat protein and LexA with the mutated version of DNA binding domain fused to the MS2 coat protein. Respectively, these two hybrid proteins specifically recognize the mutated LexA operator sequence, which contains a wild-type half-site (CTGT) and a mutated operator half-site (CTGT) described by Dimitrova et al 1998 study. This construct allows recognition of MS2-MS2-Aptazyme-PP7-PP7.

Figure: Schematic graphic of complete Aptazyme-induced bacterial three-hybrid system based on LexA heterodimer repressor

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 77
    Illegal BglII site found at 351
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 680
  • 1000
    COMPATIBLE WITH RFC[1000]