Translational_Unit

Part:BBa_K1364000:Design

Designed by: Jourdan Camille   Group: iGEM14_Toulouse   (2014-10-03)

N-acetylatedGlucosamine based chemotaxis for Bacillus subtilis


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 1913
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 1370
    Illegal SapI.rc site found at 2006


Design Notes

The chimeric protein contains the intracellular domains of McpA from Bacillus subtilis to enable the transduction of the signal: these domains correspond to the amino acids 1-37 and 282-610. The extracellular domain of VCD_000306 is inserted between the intracellular regions of McpA to sense N-acetylglucosamine and corresponds to the amino acids 31-310. Its expression is optimized for in Bacillus subtilis. This part is also composed of a Strong RBS (K780002) and a terminator (B0015) . The codon optimization was made thanks to the DNA 2.0 software program.

Chemotaxis_wo_pveg.png

Source

This gene was ordered from a synthesis company.

References

K. Meibom,L. Xibing, A. Nielsen, CY. Wu, S. Roseman and G. Schoolnik. The Vibrio cholerae chitin utilization program . The National Academy of Sciences of the USA (2004).

C. Kristich and GW. Ordal.Bacillus subtilis CheD is a chemoreceptor modification enzyme required for chemotaxis. J Biol Chem. 2002 Jul 12;277(28):25356-62. Epub 2002 May 13.