Difference between revisions of "Part:BBa K5107001"

(Functional Parameters)
 
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<partinfo>BBa_K5107001 short</partinfo>
 
<partinfo>BBa_K5107001 short</partinfo>
  
HRE5 is the 5 times repeats of th HRE minimal to increase the interaction surface of the hormone receptor with the DNA.
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Estrogen Response Element (ERE) is the consensus sequence for the binding site of the estrogen receptor<html><a href="#ref1">[1]</a></html>
  
<!-- Add more about the biology of this part here
 
===Usage and Biology===
 
  
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==Usage and Biology==
<span class='h3bb'>Sequence and Features</span>
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These inverted repeats are responsible for the interaction of the DNA Binding Domain (DBD) of the receptor with the DNA. In the human cells, these nuclear receptors work mainly as transctription activators when the hormone is present in the cytoplasm<html><a href="#ref2">[2]</a></html>. There, protein-hormone interactions trigger the translocation of the receptor to the nucleus where the transcription takes place. Because of the absence of the cofactors in the cell free system, these sites are used as operator sites, meaning that the nuclear receptor-hormone complex can bind to these and block the transcription of the upstream promoter.
<partinfo>BBa_K5107001 SequenceAndFeatures</partinfo>
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{| class="wikitable"
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|+ Human Receptor Information
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|-
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! Human Receptor !! Response Element (Operator Site) !! Natural Hormone !! Plasmid Name (In-Cell System)
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|-
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| Estrogen Receptor α (ERα) || ERE || 17β-Estradiol || pRR-ERalpha-5Z
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|-
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| Estrogen Receptor β (ERβ) || ERE || 17β-Estradiol || pRR-ERbeta-5Z
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|-
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| Glucocorticoid Receptor (GR) || HRE || Dexamethasone || pRR-GR-5Z
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|-
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| Androgen Receptor (AR) || HRE || Testosterone || pRR-AR-5Z
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|-
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| Mineralocorticoid Receptor (MR) || HRE || Aldosterone || pRR-MR-5Z
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|-
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| Progesterone Receptor (PR) || HRE || Progesterone || pRR-PR-5Z
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|}
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''Table 1: Human Receptor Information''
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The table above collect the pairs Nuclear Receptor- Response Element taken into consideariton to our project. Concerning the interaction between the receptor and DNA and after searching in the literature,it is showed that the receptor response elements do function as singular inverted repeats, but 5 tandem repeats have been proved to have a much higher effect. Previously, in-cell systems have successfully used <strong>five tandem repeats of the REs</strong> for different human hormonal receptors <html><a href="#ref3">[3]</a></html>. That is the logic behind our new composite part:[https://parts.igem.org/Part:BBa_K5107002 BBa_K5107002] and  [https://parts.igem.org/Part:BBa_K5107004 BBa_K5107004].
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===Sequence and Features===
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<partinfo>BBa_K5107001 SequenceandFeatures</partinfo>
  
  
Uncomment this to enable Functional Parameter display  
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<!-- Uncomment this to enable Functional Parameter display  
 
===Functional Parameters===
 
===Functional Parameters===
 
<partinfo>BBa_K5107001 parameters</partinfo>
 
<partinfo>BBa_K5107001 parameters</partinfo>
response element
 
 
<!-- -->
 
<!-- -->
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===References===
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<html>
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<ol>
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    <li id="ref1">
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        Miller, C. A., Tan, X., Wilson, M., Bhattacharyya, S., & Ludwig, S. (2010). 
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        Single plasmids expressing human steroid hormone receptors and a reporter gene for use in yeast signaling assays. <i>Plasmid</i>, <i>63</i>(2), 73–78. https://doi.org/10.1016/j.plasmid.2009.11.003
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    </li>
 +
    <li id="ref2">
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        Tan, M. E., Li, J., Xu, H. E., Melcher, K., & Yong, E. (2014). 
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        Androgen receptor: structure, role in prostate cancer and drug discovery. <i>Acta Pharmacologica Sinica</i>, <i>36</i>(1), 3–23. https://doi.org/10.1038/aps.2014.18
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    </li>
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    <li id="ref3">
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        Sever, R., & Glass, C. K. (2013). Signaling by nuclear receptors. <i>Cold Spring Harbor Perspectives in Biology</i>, <i>5</i>(3), a016709–a016709. https://doi.org/10.1101/cshperspect.a016709
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    </li>
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</ol>
 +
‌</html>

Latest revision as of 08:20, 30 September 2024


ERE minimal

Estrogen Response Element (ERE) is the consensus sequence for the binding site of the estrogen receptor[1]


Usage and Biology

These inverted repeats are responsible for the interaction of the DNA Binding Domain (DBD) of the receptor with the DNA. In the human cells, these nuclear receptors work mainly as transctription activators when the hormone is present in the cytoplasm[2]. There, protein-hormone interactions trigger the translocation of the receptor to the nucleus where the transcription takes place. Because of the absence of the cofactors in the cell free system, these sites are used as operator sites, meaning that the nuclear receptor-hormone complex can bind to these and block the transcription of the upstream promoter.

Human Receptor Information
Human Receptor Response Element (Operator Site) Natural Hormone Plasmid Name (In-Cell System)
Estrogen Receptor α (ERα) ERE 17β-Estradiol pRR-ERalpha-5Z
Estrogen Receptor β (ERβ) ERE 17β-Estradiol pRR-ERbeta-5Z
Glucocorticoid Receptor (GR) HRE Dexamethasone pRR-GR-5Z
Androgen Receptor (AR) HRE Testosterone pRR-AR-5Z
Mineralocorticoid Receptor (MR) HRE Aldosterone pRR-MR-5Z
Progesterone Receptor (PR) HRE Progesterone pRR-PR-5Z

Table 1: Human Receptor Information

The table above collect the pairs Nuclear Receptor- Response Element taken into consideariton to our project. Concerning the interaction between the receptor and DNA and after searching in the literature,it is showed that the receptor response elements do function as singular inverted repeats, but 5 tandem repeats have been proved to have a much higher effect. Previously, in-cell systems have successfully used five tandem repeats of the REs for different human hormonal receptors [3]. That is the logic behind our new composite part:BBa_K5107002 and BBa_K5107004.

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]


References

  1. Miller, C. A., Tan, X., Wilson, M., Bhattacharyya, S., & Ludwig, S. (2010). Single plasmids expressing human steroid hormone receptors and a reporter gene for use in yeast signaling assays. Plasmid, 63(2), 73–78. https://doi.org/10.1016/j.plasmid.2009.11.003
  2. Tan, M. E., Li, J., Xu, H. E., Melcher, K., & Yong, E. (2014). Androgen receptor: structure, role in prostate cancer and drug discovery. Acta Pharmacologica Sinica, 36(1), 3–23. https://doi.org/10.1038/aps.2014.18
  3. Sever, R., & Glass, C. K. (2013). Signaling by nuclear receptors. Cold Spring Harbor Perspectives in Biology, 5(3), a016709–a016709. https://doi.org/10.1101/cshperspect.a016709