Difference between revisions of "Part:BBa K1620004"
 
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Acts like a negative controlling element of promoter Zasp (<partinfo>BBa_K1620001</partinfo>) by use of Zn(II) as a cofactor to bind the operator of the repressed genes (znuACB). 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.
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Acts like a negative controlling element of promoter Zasp (<partinfo>BBa_K1620001</partinfo>) 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.
 
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[[Image:UFSCariGEM2015-Zur.jpg|450px|thumb|left|'''Figure 1:''' Zur protein domains.]]
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[[Image:UFSCariGEM2015-Zur.jpg|450px|thumb|center|'''Figure 1:''' Main domains of Zur protein (Fur family protein) and its zinc binding region.]]
  
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==References==
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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 coli''. '''Biochemistry''' 1987, 26:5471-5477.
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Hantke K. 1981. Regulation of ferric iron transport in ''Escherichia coli'' K12: isolation of a constitutive mutant. '''Mol. Gen. Genet.''' 182: 288-292.
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Outten CE and O'Halloran TV. 2001. Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. '''Science''' 292: 2488-2492.
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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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Latest revision as of 21:16, 13 September 2015

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 coli. Biochemistry 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.