Difference between revisions of "Part:BBa K1890001"

Revision as of 13:06, 7 September 2016

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

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.

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.

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]

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]

@@ Line 1: / Line 1: @@
 __NOTOC__
 <partinfo>BBa_K1890001 short</partinfo>
-Silicatein, originating from the demosponge Suberites domuncula, catalyzes the formation of polysilicate. The gene is fused to the transmembrane domain of outer membrane protein A (OmpA), a native protein from E. coli, together with Lpp signaling peptide.
+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>.
+<h2>References</h2>
+[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 (<i>Escherichia coli</i>) 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.
+<h2>Sequence and Features</h2>
+<partinfo>BBa_K1890001 SequenceAndFeatures</partinfo>
 <!-- Add more about the biology of this part here