Difference between revisions of "Part:BBa K1890001"
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<partinfo>BBa_K1890001 short</partinfo>
 
<partinfo>BBa_K1890001 short</partinfo>
  
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<h2>Introduction</h2>
 
Silicatein, originating from the demosponge <i>Suberites domuncula</i>, catalyzes the formation of polysilicate. This biobrick contains the short version of the silicatein gene, according to Müller <i>et al</i> [1][2]. The gene is fused to the transmembrane domain of outer membrane protein A (OmpA) together with the signaling peptide and the first nine N-terminal amino acids of lipoprotein (Lpp), both of which are native proteins from <i>Escherichia coli</i> [3]. The coding sequence in this BioBrick is combined with the strong RBS <partinfo>BBa_B0034</partinfo>.
 
Silicatein, originating from the demosponge <i>Suberites domuncula</i>, catalyzes the formation of polysilicate. This biobrick contains the short version of the silicatein gene, according to Müller <i>et al</i> [1][2]. The gene is fused to the transmembrane domain of outer membrane protein A (OmpA) together with the signaling peptide and the first nine N-terminal amino acids of lipoprotein (Lpp), both of which are native proteins from <i>Escherichia coli</i> [3]. The coding sequence in this BioBrick is combined with the strong RBS <partinfo>BBa_B0034</partinfo>.
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<h2>Sequence and Features</h2>
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<partinfo>BBa_K1890001 SequenceAndFeatures</partinfo>
  
 
<h2>References</h2>
 
<h2>References</h2>
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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.  
 
[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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===Usage and Biology===
 
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<span class='h3bb'>Sequence and Features</span>
 
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<partinfo>BBa_K1890001 SequenceAndFeatures</partinfo>
 
  
  

Revision as of 13:11, 7 September 2016

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

Introduction

Silicatein, originating from the demosponge Suberites domuncula, catalyzes the formation of polysilicate. This biobrick contains the short version of the silicatein gene, according to Müller et al [1][2]. The gene is fused to the transmembrane domain of outer membrane protein A (OmpA) together with the signaling peptide and the first nine N-terminal amino acids of lipoprotein (Lpp), both of which are native proteins from Escherichia coli [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
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 98
    Illegal NgoMIV site found at 431
  • 1000
    COMPATIBLE WITH RFC[1000]

References

[1] Müller, W. E. G., Engel, S., Wang, X., Wolf, S. E., Tremel, W., Thakur, N. L., … Schröder, H. C. (2008). Bioencapsulation of living bacteria (Escherichia coli) with poly(silicate) after transformation with silicatein-α gene. Biomaterials, 29(7), 771–779.

[2] Müller, W. E. G. (2003). Silicon biomineralization.

[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.