Difference between revisions of "Part:BBa K5107000"
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<partinfo>BBa_K5107000 short</partinfo> | <partinfo>BBa_K5107000 short</partinfo> | ||
− | + | The consensus sequence for the binding site of the human Androgen Receptor (AR), Glucocorticoid Receptor (GR), Mineralocorticoid Receptor (MR), and Progesterone receptor (PR).<html><a href="#ref1">[1]</a></html> | |
− | < | + | |
− | + | ||
− | + | ||
− | <!-- -- | + | ==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 transcription 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_K5107000 | + | |
+ | {| class="wikitable" | ||
+ | |+ 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 collects the pairs Nuclear Receptor-Response Element taken into consideration to our project. Concerning the interaction between the receptor and DNA and after searching in the literature,it is shown 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]. | ||
+ | |||
+ | ===Sequence and Features=== | ||
+ | |||
+ | <partinfo>BBa_K5107000 SequenceandFeatures</partinfo> | ||
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<partinfo>BBa_K5107000 parameters</partinfo> | <partinfo>BBa_K5107000 parameters</partinfo> | ||
<!-- --> | <!-- --> | ||
+ | ===References=== | ||
+ | <html> | ||
+ | <ol> | ||
+ | <li id="ref1"> | ||
+ | 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. <i>Plasmid</i>, <i>63</i>(2), 73–78. https://doi.org/10.1016/j.plasmid.2009.11.003 | ||
+ | </li> | ||
+ | <li id="ref2"> | ||
+ | Tan, M. E., Li, J., Xu, H. E., Melcher, K., & Yong, E. (2014). | ||
+ | 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 | ||
+ | </li> | ||
+ | <li id="ref3"> | ||
+ | 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 | ||
+ | </li> | ||
+ | </ol> | ||
+ | </html> |
Latest revision as of 17:59, 1 October 2024
HRE_minimal
The consensus sequence for the binding site of the human Androgen Receptor (AR), Glucocorticoid Receptor (GR), Mineralocorticoid Receptor (MR), and Progesterone receptor (PR).[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 transcription 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 | 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 collects the pairs Nuclear Receptor-Response Element taken into consideration to our project. Concerning the interaction between the receptor and DNA and after searching in the literature,it is shown 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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
References
- 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
- 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
- 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