Title

DNA-Induced Unfolding of the Thyroid Hormone Receptor a A/B Domain through Allostery

Source Publication

FEBS Open Bio

Authors

Elias J. Fernandez, University of Tennessee, Knoxville
Vandna Gahlot, University of Tennessee, Knoxville
Celeste Rodriguez, University of Tennessee, Knoxville
Jacob Amburn, University of Tennessee, Knoxville

Document Type

Article

Publication Date

6-5-2017

DOI

10.1002/2211-5463.12229

Abstract

The A/B domains of nuclear receptors such as thyroid receptor a (TRa) are considered to be conformationally flexible and can potentially adopt multiple structural conformations. We used intrinsic tryptophan fluorescence quenching and circular dichroism spectroscopy to characterize the unfolding of this A/B domain upon DNA binding to the contiguous DNA binding domain (DBD). We propose that this allosteric change in A/B domain conformation can allow it to make the multiple interactions with distinct molecular factors of the transcriptional preinitiation complex. We further suggest that by influencing the affinity of the DBD for DNA, A/B domain can fine-tune the recognition of promotor DNA by TRa.

Comments

This article was published openly thanks to the University of Tennessee Open Publishing Support Fund.

Licensed under a Creative Commons Attribution 4.0 International license.

Recommended Citation

Fernandez, Elias J., Vandna Gahlot, Celeste Rodriguez, and Jacob Amburn, “DNA-Induced Unfolding of the Thyroid Hormone Receptor α A/B Domain through Allostery,” FEBS Open Bio 7, no. 6 (2017), 854-864. doi: 10.1002/2211-5463.12229

Submission Type

Publisher's Version