Coding
Zur

Part:BBa_K1620004

Designed by: Celio Dias Santos Jr   Group: iGEM15_UFSCar   (2015-09-03)

Zinc uptake regulation protein - Zur

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]


Usage and Biology

Acts like a negative controlling element of promoter Zasp (BBa_K1620001) by use of Zn2+ as a cofactor to bind the operator of the repressed genes (znuACB). Fur (ferric uptake regulator) family proteins regulate metal homeostasis and oxidative stress responses (Bagg & Neilands, 1987; Hantke 1981). In E. coli, Zur is known to exhibit sensitivity to femtomolar levels of free intracellular zinc (Outten & O’Halloran) and regulates the high-affinity zinc uptake system ZnuACB (Patzer & Hantke). In our project it was used to regulate a kill switch based on zinc concentration to promote cellular death. Its main domains are shown in Figure 1.

Figure 1: Main domains of Zur protein (Fur family protein) and its zinc binding region.

References

Bagg A and Neilands JB. 1987. Ferric uptake regulation protein acts as a repressor, employing iron(II) as a cofactor to bind the operator of an iron transport operon in Escherichia coliBiochemistry 1987, 26:5471-5477.

Hantke K. 1981. Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant. Mol. Gen. Genet. 182: 288-292.

Outten CE and O'Halloran TV. 2001. Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292: 2488-2492.

Patzer SI and Hantke K. 2000. The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli. J. Biol. Chem. 275: 24321-24332.

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