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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==Usage and Biology==
  
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<!-- Add more about the biology of this part here
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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. For JUMP assembly, this part is designed as a O part.
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===Usage and Biology===
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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. [Online] 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.). [Online] 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. [Online] 222112512–112512.
  
  

Revision as of 16:00, 8 October 2022


SUMO tag :: Glycine-Serine Linker

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. For JUMP assembly, this part is designed as a O part.

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. [Online] 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.). [Online] 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. [Online] 222112512–112512.