Part:BBa_K1189024
Light chain human ferritin
This part is the light ferritin subunit from human ferritin, inspired by P02792 [UniParc]. Ferritin is ubiquitous across prokaryotic and eukaryotic systems and is used to buffer intracellular iron. This part, along with the heavy ferritin subunit, form a 24 multimeric iron sequestering nanoparticle (Chasteen et al., 1991). The light ferritin purportedly contributes to nucleation to initiate iron core formation in ferritin molecules (Chasteen et al., 1999). These nanoparticles are robust, remain stable at extreme pHs, and withstand temperature variations (Kim et al., 1999).
Figure 1. Ribbon visualization of a fully assembled ferritin protein.
Ferritin's utility in iGEM
Ferritin as a nanoparticle is interesting for other iGEM teams for two reasons. Firstly, its iron core can be replaced with other compounds to serve different functions. The iGEM Calgary 2013 demonstrated this by chemically modifying recombinant ferritin's iron core into a robust colourmetric reporter. Other intriguing applications include making ferritin’s iron core magnetically active as magnetoferritin (Jordan et al. 2013), using ferritin as a nanocage for other metals, or the incorporation of other reporters such as quantum dots (Naito et al. 2013) (Figure 2).
Figure 2. Chemically modifying the iron core of ferritin allows ferritin to be moulded to fit a wide magnitude of applications. Additionally the ferritin subunits can act as a nanocage to encapsulate completely new cores.
Secondly, the ferritin nanoparticle is useful for iGEM teams as a self-assembling and spherical protein scaffold. Each of the 24 subunits forming ferritin can be fused to proteins of interest, such that when the nanoparticle assembles, proteins surround the ferritin sphere (Kim et al., 2011). The iGEM Calgary 2013 team demonstrated this by binding DNA sensing proteins, TALEs, as part of their FerriTALE sensor. The Calgary team also constructed ferritin subunits with a coiled-coil linker system so that other teams can scaffold proteins to E-coil ferritin (BBa_K1189018, BBa_K1189019, BBa_K1189020, BBa_K1189037). See Figure 3 for a demonstration of these applications.
Figure 3. Using the E and K coils in combination with ferritin as a scaffold system allows the creation of brand new FerriTALEs or protein scaffolds.
References
Chasteen, N. D., & Harrison, P. M. (1999). Mineralization in ferritin: an efficient means of iron storage. Journal of structural biology, 126(3), 182-194.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 391
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