Difference between revisions of "Part:BBa K2324002"
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The literature has shown that the terminal pili protein FimH (Le Trong et al 2010) can be modified by inserting heterologous sequences at position 225 and 258 (Pallesen et al 1995, Shembri et al 1999). However these two amino acids are in the pilin binding domain which may present difficulties when attempting to introduce large modifications. Harvard iGEM 2015 also introduced modifications at position 1 of the mature FimH protein.</p> | The literature has shown that the terminal pili protein FimH (Le Trong et al 2010) can be modified by inserting heterologous sequences at position 225 and 258 (Pallesen et al 1995, Shembri et al 1999). However these two amino acids are in the pilin binding domain which may present difficulties when attempting to introduce large modifications. Harvard iGEM 2015 also introduced modifications at position 1 of the mature FimH protein.</p> | ||
<p> | <p> | ||
| − | This part tests expression and folding of FimH. Fluorescence suggests both that the protein is sufficiently folded such that the sfGFP works. Other techniques can then be used to demonstrate successful pilus biosynthesis. </p> | + | This part tests expression and folding of FimH. Fluorescence suggests both that the protein is sufficiently folded such that the sfGFP works. Other techniques can then be used to demonstrate successful pilus biosynthesis. It is included in the composite part https://parts.igem.org/Part:BBa_K2324007 under the pRha promoter. </p> |
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Revision as of 19:56, 1 November 2017
FimH+sfGFP at residue 1
The literature has shown that the terminal pili protein FimH (Le Trong et al 2010) can be modified by inserting heterologous sequences at position 225 and 258 (Pallesen et al 1995, Shembri et al 1999). However these two amino acids are in the pilin binding domain which may present difficulties when attempting to introduce large modifications. Harvard iGEM 2015 also introduced modifications at position 1 of the mature FimH protein.
This part tests expression and folding of FimH. Fluorescence suggests both that the protein is sufficiently folded such that the sfGFP works. Other techniques can then be used to demonstrate successful pilus biosynthesis. It is included in the composite part https://parts.igem.org/Part:BBa_K2324007 under the pRha promoter.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]