Difference between revisions of "Part:BBa K4882007"

 
 
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<partinfo>BBa_K4882007 short</partinfo>
 
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This part linked the MCL1 signal peptide to the LqhIT2 insect-specific toxin. The signal peptide guides the toxin to be secreted.
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This is an Mcl1 secretory signal peptide fused with an insect-specific toxin LqhIT2.  
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===Usage and Biology===
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<partinfo>BBa_K4882007 parameters</partinfo>
 
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===Usage and Biology===
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The Mcl1 signal peptide (Mcl1ss, [https://parts.igem.org/Part:BBa_K4882002 BBa_K4882002]) is from the collagen-like protein MCL1 of Metarhizium anisopliae. Mcl1ss is an 18-amino acid secretory signal peptide at the N-terminus of the MCL1 protein.
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LqhIT2 ([https://parts.igem.org/Part:BBa_K4882001 BBa_K4882001]) is a 61 amino acid-long scorpion depressant toxin from L. quinquestriatus hebraeus. Although the scorpion is dangerous to humans, LqhIT2 is not. LqhIT2 shows a high preference for insect voltage-gated sodium channels and is totally harmless to mammals.
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To improve the efficiency of M. anisopliae as a fungal biopesticide, we choose to introduce the LqhIT2 toxin into the fungus. To promote the secretion of the toxin, a Mcl1ss is linked at the 5’ end of the LqhIT2 gene.

Latest revision as of 14:50, 4 October 2023


Mcl1 signal peptide-LqhIT2

This is an Mcl1 secretory signal peptide fused with an insect-specific toxin LqhIT2.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 145
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]



Usage and Biology

The Mcl1 signal peptide (Mcl1ss, BBa_K4882002) is from the collagen-like protein MCL1 of Metarhizium anisopliae. Mcl1ss is an 18-amino acid secretory signal peptide at the N-terminus of the MCL1 protein.

LqhIT2 (BBa_K4882001) is a 61 amino acid-long scorpion depressant toxin from L. quinquestriatus hebraeus. Although the scorpion is dangerous to humans, LqhIT2 is not. LqhIT2 shows a high preference for insect voltage-gated sodium channels and is totally harmless to mammals.

To improve the efficiency of M. anisopliae as a fungal biopesticide, we choose to introduce the LqhIT2 toxin into the fungus. To promote the secretion of the toxin, a Mcl1ss is linked at the 5’ end of the LqhIT2 gene.