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首页> 外文期刊>Journal of Molecular Biology >Conformational Changes of ROR gamma During Response Element Recognition and Coregulator Engagement
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Conformational Changes of ROR gamma During Response Element Recognition and Coregulator Engagement

机译：Conformational Changes of ROR gamma During Response Element Recognition and Coregulator Engagement

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The retinoic acid receptor-related orphan receptor gamma (ROR gamma) is a ligand-dependent transcription factor of the nuclear receptor super family that underpins metabolic activity, immune function, and cancer progression. Despite being a valuable drug target in health and disease, our understanding of the ligand-dependent activities of ROR gamma is far from complete. Like most nuclear receptors, ROR gamma must recruit coregulatory protein to enact the ROR gamma target gene program. To date, a majority of structural studies have been focused exclusively on the ROR gamma ligand-binding domain and the ligand-dependent recruitment of small peptide segments of coregulators. Herein, we examine the ligand-dependent assembly of full length ROR gamma:coregulator complexes on cognate DNA response elements using structural proteomics and small angle x-ray scattering. The results from our studies suggest that ROR gamma becomes elongated upon DNA recognition, preventing long range interdomain crosstalk. We also determined that the DNA binding domain adopts a sequence-specific conformation, and that coregulatory protein may be able to 'sense' the ligand- and DNA-bound status of ROR gamma. We propose a model where ligand-dependent coregulator recruitment may be influenced by the sequence of the DNA to which ROR gamma is bound. Overall, the efforts described herein will illuminate important aspects of full length ROR gamma and monomeric orphan nuclear receptor target gene regulation through DNA-dependent conformational changes. (C) 2021 Elsevier Ltd. All rights reserved.

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