DNA-induced unfolding of the thyroid hormone receptor α A/B domain through allostery.

Abstract:

:The A/B domains of nuclear receptors such as thyroid receptor α (TRα) 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 TRα.

journal_name

FEBS Open Bio

journal_title

FEBS open bio

authors

Fernandez EJ,Gahlot V,Rodriguez C,Amburn J

doi

10.1002/2211-5463.12229

subject

Has Abstract

pub_date

2017-05-15 00:00:00

pages

854-864

issue

6

issn

2211-5463

pii

FEB412229

journal_volume

7

pub_type

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