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Monitoring Estrogen Receptor Dimerization via Bipartite Tetracysteine Display

Tang, Tang
http://orcid.org/0000-0002-1632-0370
http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1562622108928366

Abstract Details

2019, Master of Science (MS), Ohio University, Chemistry and Biochemistry (Arts and Sciences).
The human estrogen receptor (hER) is a ligand-mediated transcription factor that plays a critical role in cell growth, differentiation and development. In the classical model of hER signaling, estrogenic ligands such as 17$\beta$-estradiol initiate estrogen receptors to form ligand-bound dimers, which then translocate into the nucleus, bind to estrogen response elements on DNA and modulate gene expression. As dimer formation is thought to be essential for normal receptor function, there is considerable interest in studying ligand-mediated estrogen receptor dimerization. However, the ability for researchers to monitor ligand-mediated ER dimerization in real time is limited. In this research project, a small molecule biarsenical profluorophore, $\text{FlAsH-EDT}_2$ was employed to study how the formation of estrogen receptor dimerization is affected by estrogenic compounds \textit{in vitro}. $\text{FlAsH-EDT}_2$ is nonfluorescent until it binds to a tetracysteine (C4) motif within protein or peptide, whereupon it becomes strongly fluorescent. In this research, we developed hER mutants containing two cysteine residues at different positions along their dimerization interface. Upon ligand-induced dimerization, a tetracysteine motif that can be bound by $\text{FlAsH-EDT}_2$ is formed between the two estrogen receptors. Because the $\text{FlAsH-EDT}_2$ molecule only becomes fluorescent upon binding a C4 motif, it will allow for quantification of estrogen receptor dimerization as a function of fluorescent intensity.
Justin Holub (Advisor)
Shiyong Wu (Committee Member)
Travis White (Committee Member)
89 p.
Biochemistry
Biarsenicals; estrogen receptor dimerization; estradiol

Recommended Citations

Citations

  • Tang, T. (2019). Monitoring Estrogen Receptor Dimerization via Bipartite Tetracysteine Display [Master's thesis, Ohio University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1562622108928366

    APA Style (7th edition)

  • Tang, Tang. Monitoring Estrogen Receptor Dimerization via Bipartite Tetracysteine Display. 2019. Ohio University, Master's thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1562622108928366.

    MLA Style (8th edition)

  • Tang, Tang. "Monitoring Estrogen Receptor Dimerization via Bipartite Tetracysteine Display." Master's thesis, Ohio University, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1562622108928366

    Chicago Manual of Style (17th edition)

ohiou1562622108928366
392
© 2019, all rights reserved.
This open access ETD is published by Ohio University and OhioLINK.