Difference between revisions of "Part:BBa K2871000:Design"

(Source)
(Design Notes)
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===Design Notes===
 
===Design Notes===
The paper described by Charpentier & Oswald (2004), showed that a 20 amino acid sequence was sufficient albeit not the best. The short length however seemed attractive to us, because we wanted to minimize folding interference between the signal sequence and the intended protein fused to the signal sequence.
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The paper described by Charpentier & Oswald (2004), showed that a 20 amino acid signal sequence of Map protein was sufficient for translocation via E. coli T3SS. The short length signal sequence seemed attractive to us because we wanted to minimize folding interference between the signal sequence and the intended protein fused to the signal sequence.
 
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===Source===
 
===Source===

Revision as of 19:10, 7 October 2018


Map20, T3SS export signal peptide from Map gene


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Unknown
  • 23
    INCOMPATIBLE WITH RFC[23]
    Unknown
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 85
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

The paper described by Charpentier & Oswald (2004), showed that a 20 amino acid signal sequence of Map protein was sufficient for translocation via E. coli T3SS. The short length signal sequence seemed attractive to us because we wanted to minimize folding interference between the signal sequence and the intended protein fused to the signal sequence.

Source

Synthetic sequence deduced from Amino acid Sequence from the Enteropathogenic E. coli strain E22. Described in the paper Charpentier & Oswald, 2004.

References

Charpentier & Oswald, 2004. journal of baceteriology. 'Identification of the Secretion and Translocation Domain of the Enteropathogenic and Enterohemorrhagic Escherichia coli Effector Cif, Using TEM-1 β-Lactamase as a New Fluorescence-Based Reporter' DOI: 10.1128/JB.186.16.5486-5495.2004 https://jb.asm.org/content/186/16/5486