Difference between revisions of "Part:BBa K1890002"

 
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<partinfo>BBa_K1890002 short</partinfo>
 
<partinfo>BBa_K1890002 short</partinfo>
  
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Silicatein, originating from the demosponge Tethya aurantia, catalyzes the formation of polysilicate. As described by Curnow et al, the silicatein gene was fused to the transmembrane domain of outer membrane protein A (OmpA), in order to display it at the surface of the cell. The fusion of silicatein and OmpA is constructed according to Francisco et al, consisting of the transmembrane domain of OmpA together with the signaling peptide and the first nine N-terminal amino acids of lipoprotein (Lpp). The coding sequence in this BioBrick is combined with the strong RBS.
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<h2>Introduction</h2>
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Silicatein, originating from the demosponge <i>Tethya aurantia</i>, catalyzes the formation of polysilicate.  
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As described by Curnow <i>et al</i>, the silicatein gene was fused to the transmembrane domain of outer membrane  
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protein A (OmpA), in order to display it at the surface of the cell [1][2].  
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The fusion of silicatein and OmpA is constructed according to Francisco <i>et al</i>,  
 +
consisting of the transmembrane domain of OmpA together with the signaling peptide and the first  
 +
nine N-terminal amino acids of lipoprotein (Lpp) [3]. The coding sequence in this BioBrick is  
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combined with the strong RBS <partinfo>BBa_B0034</partinfo>.
  
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<h2>Sequence and Features</h2>
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===Usage and Biology===
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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K1890002 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K1890002 SequenceAndFeatures</partinfo>
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<h2>References</h2>
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[1] Curnow, P., Kisailus, D., & Morse, D. E. (2006). Biocatalytic synthesis of poly(L-lactide) by native and recombinant forms of the silicatein enzymes. Angewandte Chemie - International Edition, 45(4), 613–616.
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[2] Curnow, P., Bessette, P. H., Kisailus, D., Murr, M. M., Daugherty, P. S., & Morse, D. E. (2005). Enzymatic synthesis of layered titanium phosphates at low temperature and neutral pH by cell-surface display of silicatein-?? Journal of the American Chemical Society, 127(45), 15749–15755.
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[3] Francisco, J. a, Earhart, C. F., & Georgiou, G. (1992). Transport and anchoring of beta-lactamase to the external surface of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, 89(April), 2713–2717.
  
  
 
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===Functional Parameters===
 
===Functional Parameters===
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<partinfo>BBa_K1890002 parameters</partinfo>
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<partinfo>BBa_K1890001 parameters</partinfo>
 
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Revision as of 16:03, 8 September 2016

Silicatein gene, fused to transmembrane domain of OmpA, with strong RBS

Introduction

Silicatein, originating from the demosponge Tethya aurantia, catalyzes the formation of polysilicate. As described by Curnow et al, the silicatein gene was fused to the transmembrane domain of outer membrane protein A (OmpA), in order to display it at the surface of the cell [1][2]. The fusion of silicatein and OmpA is constructed according to Francisco et al, consisting of the transmembrane domain of OmpA together with the signaling peptide and the first nine N-terminal amino acids of lipoprotein (Lpp) [3]. The coding sequence in this BioBrick is combined with the strong RBS BBa_B0034.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 192
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]

References

[1] Curnow, P., Kisailus, D., & Morse, D. E. (2006). Biocatalytic synthesis of poly(L-lactide) by native and recombinant forms of the silicatein enzymes. Angewandte Chemie - International Edition, 45(4), 613–616.

[2] Curnow, P., Bessette, P. H., Kisailus, D., Murr, M. M., Daugherty, P. S., & Morse, D. E. (2005). Enzymatic synthesis of layered titanium phosphates at low temperature and neutral pH by cell-surface display of silicatein-?? Journal of the American Chemical Society, 127(45), 15749–15755.

[3] Francisco, J. a, Earhart, C. F., & Georgiou, G. (1992). Transport and anchoring of beta-lactamase to the external surface of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, 89(April), 2713–2717.