Difference between revisions of "Part:BBa K4634000"
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pPepT, which is induced by hypoxia, is regulated by transcriptional activator: fumarate and nitrate reduction regulatory protein (FNR).[1]Under anaerobic conditions, FNR associates with [4Fe-4S]2+ clusters to form transcriptionally active homodimers, the dimer can bind  DNA  site-specifically  and  regulate  transcription  from  target promoters. However, when the clusters are disrupted in the presence of oxygen, the FNR dimer dissociates into nonDNA-binding monomers. [2, 3]
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pPepT, which is induced by hypoxia, is regulated by transcriptional activator: fumarate and nitrate reduction regulatory protein (FNR)(Fig. 1).[1]Under anaerobic conditions, FNR associates with [4Fe-4S]2+ clusters to form transcriptionally active homodimers, the dimer can bind  DNA  site-specifically  and  regulate  transcription  from  target promoters. However, when the clusters are disrupted in the presence of oxygen, the FNR dimer dissociates into nonDNA-binding monomers. [2, 3]
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<center><html><img src='https://static.igem.wiki/teams/4634/wiki/parts-registry/bba-k4634000.png' width='400px'></html></center>
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<center><html>Figure 1. Regulatory mechanism of hypoxia-inducible promoter pPepT.
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Under normoxic conditions, FNR monomer cannot dimerize and cannot promote the regulatory function of pPepT. It can be regarded that oxygen inhibits the function of pPepT. Under hypoxic conditions, FNR monomers can interact to form dimers, which can specifically bind to pPepT and promote the transcription of its downstream genes.
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===References===
 
===References===

Revision as of 15:18, 3 October 2023


pPepT: hypoxia-inducible promoter

pPepT, which is induced by hypoxia, is regulated by transcriptional activator: fumarate and nitrate reduction regulatory protein (FNR)(Fig. 1).[1]Under anaerobic conditions, FNR associates with [4Fe-4S]2+ clusters to form transcriptionally active homodimers, the dimer can bind DNA site-specifically and regulate transcription from target promoters. However, when the clusters are disrupted in the presence of oxygen, the FNR dimer dissociates into nonDNA-binding monomers. [2, 3]


Figure 1. Regulatory mechanism of hypoxia-inducible promoter pPepT. Under normoxic conditions, FNR monomer cannot dimerize and cannot promote the regulatory function of pPepT. It can be regarded that oxygen inhibits the function of pPepT. Under hypoxic conditions, FNR monomers can interact to form dimers, which can specifically bind to pPepT and promote the transcription of its downstream genes.


References

[1]Yu, Bin, et al. "Explicit hypoxia targeting with tumor suppression by creating an “obligate” anaerobic Salmonella Typhimurium strain." Scientific reports 2.1 (2012): 436.

[2]Crack, Jason C., et al. "Signal perception by FNR: the role of the iron sulfur cluster1." (2008): 1144-1148.

[3] CRACK J C, GASKELL A A, GREEN J, et al. Influence of the Environment on the [4Fe−4S]2+ to [2Fe−2S]2+ Cluster Switch in the Transcriptional Regulator FNR [J]. Journal of the American Chemical Society, 2008, 130(5): 1749-58.


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]