Difference between revisions of "Part:BBa K4390017"

 
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<partinfo>BBa_K4390017 short</partinfo>
 
<partinfo>BBa_K4390017 short</partinfo>
  
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This part adds a SUMO tag separated by a Glycine-Serine linker. We used this part for increased Metallothionein stability in cells during directed evolution of metallothioneins.  
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'''This part is not compatible with BioBrick RFC10 assembly but is compatible with the iGEM Type IIS Part standard [[Help:Standards/Assembly/Type_IIS|which is also accepted by iGEM.]]'''
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'''This is a Level 0 part of type O part generating the following 4 base overhangs at upstream (AGCC) and downstream (TTCG) ends.'''
  
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<!-- Add more about the biology of this part here
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==Usage and Biology==
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===Usage and Biology===
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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.
  
 
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<span class='h3bb'>Sequence and Features</span>
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==<span class='h3bb'>Sequence and Features</span>==
 
<partinfo>BBa_K4390017 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4390017 SequenceAndFeatures</partinfo>
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==References==
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Henley, J. M. et al. (2007) SUMOylation regulates kainate-receptor-mediated synaptic transmission. Nature. 447 (7142), 321–325.
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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.
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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.
  
  

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


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE 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.