Difference between revisions of "Part:BBa K4882007"

Revision as of 13:48, 4 October 2023

Mcl1 signal peptide-LqhIT2

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

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.

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]

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 <partinfo>BBa_K4882007 short</partinfo>
-This part linked the MCL1 signal peptide to the LqhIT2 insect-specific toxin. The signal peptide guides the toxin to be secreted.
+This is an Mcl1 secretory signal peptide fused with an insect-specific toxin LqhIT2.
-<!-- Add more about the biology of this part here
+<!-- Add more about the biology of this part here-->
 ===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.
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