Difference between revisions of "Part:BBa K1679020"
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This is a translational unit containing a RBS (BBa_B0034) and a [https://parts.igem.org/Part:BBa_K1679029 ftnA] on the pSB1C3. | This is a translational unit containing a RBS (BBa_B0034) and a [https://parts.igem.org/Part:BBa_K1679029 ftnA] on the pSB1C3. | ||
| − | === | + | ===Ferritin=== |
FtnA is a bacterial ferritin with a protein shell is assembled from 24 identical 19.4 kDa FtnA monomers. Its central cavity is around 7.5 nm in diameter and can be loaded with iron when cells grow under iron-rich | FtnA is a bacterial ferritin with a protein shell is assembled from 24 identical 19.4 kDa FtnA monomers. Its central cavity is around 7.5 nm in diameter and can be loaded with iron when cells grow under iron-rich | ||
conditions[1]. The iron is stored in the form of ferrihydrite iron cores normally that with superparamagnetic properties[2]. The iron contained ferritin can generate heat in response to electromagnetic signal[3]. For the reasons above, we design it as our magnetic receiver which can turn electromagnetic signal into heat. | conditions[1]. The iron is stored in the form of ferrihydrite iron cores normally that with superparamagnetic properties[2]. The iron contained ferritin can generate heat in response to electromagnetic signal[3]. For the reasons above, we design it as our magnetic receiver which can turn electromagnetic signal into heat. | ||
Revision as of 19:12, 18 September 2015
RBS+ftnA
This is a translational unit containing a RBS (BBa_B0034) and a ftnA on the pSB1C3.
Ferritin
FtnA is a bacterial ferritin with a protein shell is assembled from 24 identical 19.4 kDa FtnA monomers. Its central cavity is around 7.5 nm in diameter and can be loaded with iron when cells grow under iron-rich conditions[1]. The iron is stored in the form of ferrihydrite iron cores normally that with superparamagnetic properties[2]. The iron contained ferritin can generate heat in response to electromagnetic signal[3]. For the reasons above, we design it as our magnetic receiver which can turn electromagnetic signal into heat.
[1]Smith J L. The physiological role of ferritin-like compounds in bacteria[J]. Critical reviews in microbiology, 2004, 30(3): 173-185. [2] Papaefthymiou G C, Viescas A J, Devlin E, et al. Electronic and magnetic characterization of in vivo produced vs. in vitro reconstituted horse spleen ferritin[C]//MRS Proceedings. Cambridge University Press, 2007, 1056: 1056-HH03-27. [3] Stanley S A, Sauer J, Kane R S, et al. Remote regulation of glucose homeostasis in mice using genetically encoded nanoparticles[J]. Nature medicine, 2015, 21(1): 92-98.
Experiment
We purified the ferritin overexpressed in E.coli through Ni-chelating affinity chromatography and highly concentrated it and then do SDS-PAGE. The position of clearly targeted band(about 19.4kDA) on the gel was consistent with the size of ferritin monomer fused with tag on plasmid, explaining that the ftnA expression is successful.
Gel was stained with (A) potassium ferrocyanide and (B) Coomassie Brilliant Blue R250. Control, HFn; lane 1, concentrated mineralized ferritin purified product; lane 2, sediment of bacteria with mineralization; lane 3, concentrated unmineralized ferritin purified product ; lane 4, sediment of bacteria without mineralization.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]