Difference between revisions of "Part:BBa K2324010"
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<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>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 produces a FimH adhesin protein fused with a metallothionein from <i>Mus musculus</i> at the first amino acid position. The coding sequence is under the control of a rhamnose-inducible promoter, with a B0034 RBS and a B0015 terminator. The part, when induced, produces a metal binding FimH protein that should initiates pilus biosynthesis when co-transformed with a plasmid containing the <i>fim operon</i></p> . | + | This part produces a FimH adhesin protein fused with a metallothionein from <i>Mus musculus</i> (Huang et al 1981) at the first amino acid position, after signal peptide cleavage. The coding sequence is under the control of a rhamnose-inducible promoter, with a B0034 RBS and a B0015 terminator. The part, when induced, produces a metal binding FimH protein that should initiates pilus biosynthesis when co-transformed with a plasmid containing the <i>fim operon</i></p> . |
Revision as of 22:03, 1 November 2017
pRha_FimH_1MouseMT
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 produces a FimH adhesin protein fused with a metallothionein from Mus musculus (Huang et al 1981) at the first amino acid position, after signal peptide cleavage. The coding sequence is under the control of a rhamnose-inducible promoter, with a B0034 RBS and a B0015 terminator. The part, when induced, produces a metal binding FimH protein that should initiates pilus biosynthesis when co-transformed with a plasmid containing the fim operon
.
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]