A fusion protein of a transmembrane domain (Lpp-OmpA) and a zinc-finger domain (sZF10),under pL_lac promotion and containing a C-terminal FLAG tag. It is used to exhibit a zinc-finger dsDNA binding domain complimentary to TGCTGCTTC on the cell surface of E.coli.
Lpp-OmpA is originally from E.coli; sZF10 is from http://www.nature.com/nmeth/journal/v10/n5/abs/nmeth.2407.html
We had to optimise the codon for E.coli K12, and then alter the codon slightly to remove unwanted cut sites. The Lpp-OmpA domain is preceeded by an NdeI cut site, and followed by an AgeI cut site. The sZF10 domain is preceeded by an NheI cut site and followed by a ClaI cut site.
A fusion protein of a transmembrane domain (BclA) and a zinc-finger domain (Zif268 1AAY fragment),under pL_lac promotion and containing a C-terminal FLAG tag. It is used to exhibit a zinc-finger dsDNA binding domain complimentary to CCGCCCNCGC on the cell surface of E.coli.
We had to optimise the codon for E.coli K12, and then alter the codon slightly to remove unwanted cut sites. The BclA domain is preceeded by an NdeI cut site, and followed by an AgeI cut site. The Zif268 fragment domain is preceeded by an NheI cut site and followed by a ClaI cut site.
BclA is originally from Bacillus Anthracis; Zif268 is from mice.
A fusion protein of a transmembrane domain (Lpp-OmpA) and a zinc-finger domain (sZF14),under pL_lac promotion and containing a C-terminal FLAG tag. It is used to exhibit a zinc-finger dsDNA binding domain complimentary to TCCTCACTC on the cell surface of E.coli.
We had to optimise the codon for E.coli K12, and then alter the codon slightly to remove unwanted cut sites. The Lpp-OmpA domain is preceeded by an NdeI cut site, and followed by an AgeI cut site. The sZF14 domain is preceeded by an NheI cut site and followed by a ClaI cut site.
Lpp-OmpA is originally from E.coli; sZF2 is from http://www.nature.com/nmeth/journal/v10/n5/abs/nmeth.2407.html
trkD, a functional Kup (formerly TrkD) system took up Cs+ with a moderate rate and affinity
Escherichia coli cells which contain a functional Kup (formerly TrkD) system took up Cs' with a moderate rate and affinity. Kup is a separate K+ uptake system with relatively little discrimination in the transport of the cations K+, Rb+, and Cs'. Regardless of the presence or absence of Kup, K+-replete cells took up Cs'primarily by a very low affinity mode, proportional to the ratio of the Cs' and K+ concentrations in the medium. In our project, trkD is used to collect Cs-137 when recN is activated by radiation and start the transcription of trkD,in order to absorb this kind of radioactive source like Cs-137
A fusion protein of a transmembrane domain (Lpp-OmpA) and a zinc-finger domain (sZF2),under pL_lac promotion and containing a C-terminal FLAG tag. It is used to exhibit a zinc-finger dsDNA binding domain complimentary to TGCTGCTTC on the cell surface of E.coli.
We had to optimise the codon for E.coli K12, and then alter the codon slightly to remove unwanted cut sites. The Lpp-OmpA domain is preceeded by an NdeI cut site, and followed by an AgeI cut site. The sZF2 domain is preceeded by an NheI cut site and followed by a ClaI cut site.
A fusion protein of a transmembrane domain (Lpp-OmpA) and a zinc-finger domain (Zif268 1AAY fragment),under pL_lac promotion and containing a C-terminal FLAG tag. It is used to exhibit a zinc-finger dsDNA binding domain complimentary to CCGCCCNCGC on the cell surface of E.coli.
We had to optimise the codon for E.coli K12, and then alter the codon slightly to remove unwanted cut sites.
Lpp-OmpA is originally from E.coli; Zif268 is from mice.
Transmembrane region of the EGF-Receptor (ErbB-1)
Helical, single-span transmembrane region of the human EGF-Receptor type ErbB-1, sequence taken from UniProtKB/Swiss-Prot entry P00533.
Between BioBrick 1.0 sites this part is flanked 5' by NgoMI(=NgoMIV) and 3' AgeI(=PinAI) to facilitate in frame cloning for protein fusions.
Transmembrane region of the human EGF-Receptor type ErbB-1. Sequence taken from UniProtKB/Swiss-Prot entry P00533. Gene synthesis by ATG:biosynthetics, optimized for expression in homo sapiens by iGEM-Team Freiburg 2008.
This gene encodes the terephthalic acid(TPA) transporting protein. TPA is not a kind of nutrient substance for most organisms, including common chassis organisms like E.coli and Saccharomyces cerevisiae. However, as a kind of TPA degradable organism, RhodococcusjostiiRHA1 can transport TPA into their cells because of the TPA transporting protein genetpaK in their genome. This gene is also verified to be useful in Saccharomyces cerevisiae.
It comes from the genome of RhodococcusjostiiRHA1.
A fusion protein of a transmembrane domain (INP) and a zinc-finger domain (Zif268 1AAY fragment),under pL_lac promotion and containing a C-terminal FLAG tag. It is used to exhibit a zinc-finger dsDNA binding domain complimentary to CCGCCCNCGC on the cell surface of E.coli.
We had to optimise the codon for E.coli K12, and then alter the codon slightly to remove unwanted cut sites. The INP domain is preceeded by an NdeI cut site, and followed by an AgeI cut site. The Zif268 fragment domain is preceeded by an NheI cut site and followed by a ClaI cut site.
Lpp-OmpA is originally from Pseudomonas syringae; Zif268 is from mice.
We have to optimizes its codons in Arabidopsis Thaliana and removed the restriction sites for EcoR1, Xba1, Spe1 and Pst1.
EnvZ Signal Peptide and first Transmembrane Domain
For EnvZ fusion protein design. Long description will be added soon.
Source: E. coli EnvZ protein (ncbi: https://www.ncbi.nlm.nih.gov/gene/947272)
EnvZ-LRR chimeric receptor for mDAP recognition
EnvZ Signal Transduction and Kinase Domains
E. coli EnvZ (ncbi: https://www.ncbi.nlm.nih.gov/gene/947272)