Difference between revisions of "Part:BBa K4390017"
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==<span class='h3bb'>Sequence and Features</span>== | ==<span class='h3bb'>Sequence and Features</span>== | ||
<partinfo>BBa_K4390017 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4390017 SequenceAndFeatures</partinfo> |
Latest revision as of 23:19, 13 October 2022
SUMO tag :: Glycine-Serine Linker
This part is not compatible with BioBrick RFC10 assembly but is compatible with the iGEM Type IIS Part standard which is also accepted by iGEM. This is a Level 0 part of type O part generating the following 4 base overhangs at upstream (AGCC) and downstream (TTCG) ends.
Usage and Biology
SUMO tag is a small protein with around 12 kDa. When expressing desired protein in E. coli, most protein will be insoluble which cause aggregation or instability. One solution to this situation is the fusion of desired protein with different tags or proteins which can increase the solubility. This part is a SUMO tag with a Glycine-Serine (GS) linker added at the 3’ end. SUMO tag is important to keep the stability (Henley, J. M. et al., 2007) and increase the solubility (Kuo, D. et al., 2014) in both prokaryote and eukaryote. The GS linker will be used to fuse the SUMO with metallothionein (Li, X. et al., 2021) to increase the protein stability and solubility in E. coli.
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]
References
Henley, J. M. et al. (2007) SUMOylation regulates kainate-receptor-mediated synaptic transmission. Nature. 447 (7142), 321–325.
Kuo, D. et al. (2014) SUMO as a Solubility Tag and In Vivo Cleavage of SUMO Fusion Proteins with Ulp1. Methods in molecular biology (Clifton, N.J.). 117771–80.
Li, X. et al. (2021) Genetic modifications of metallothionein enhance the tolerance and bioaccumulation of heavy metals in Escherichia coli. Ecotoxicology and environmental safety. 222112512–112512.