Difference between revisions of "Part:BBa K2324003"

Revision as of 19:53, 1 November 2017

FimH+sfGFP at residue 258

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 258 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.

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]

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 __NOTOC__
 <partinfo>BBa_K2324003 short</partinfo>
+<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.
+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 258 of the mature FimH protein.</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>
 <!-- Add more about the biology of this part here