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Nucleosome Engagement Regulates RORγt Structure and Dynamics.

Timothy S Strutzenberg1, Matthew D Mann2, Xiandu Li1

  • 1The Salk Institute for Biological Studies, La Jolla, CA, USA.

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Summary
This summary is machine-generated.

Retinoic acid-related orphan receptor gamma (RORγt) binding to DNA is influenced by nucleosomes. This study reveals how RORγt interacts with chromatin to regulate gene expression in immune cells.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Structural Biology

Background:

  • Retinoic acid-related orphan receptor gamma (RORγt) is crucial for Th17 cell development and immune responses.
  • RORγt binds DNA response elements to activate gene expression, but its interaction with chromatin is not well understood.

Purpose of the Study:

  • To investigate how the nucleosome, a fundamental unit of chromatin, affects RORγt binding, structure, and function.
  • To elucidate the mechanisms by which RORγt interacts with chromatinized DNA to regulate gene expression.

Main Methods:

  • Nucleosome accessibility profiling to determine RORγt binding sites on DNA.
  • Hydrogen deuterium exchange coupled with mass spectrometry (HDX-MS) to study RORγt dynamics and allosteric effects.
  • High-resolution structural analysis of RORγt bound to nucleosomes.

Main Results:

  • RORγt preferentially binds to free DNA and nucleosome entry/exit sites with single base-pair resolution.
  • Allosteric effects influencing RORγt binding and chromatin dynamics were identified.
  • A high-resolution structure revealed how RORγt specifically binds to chromatin substrates.

Conclusions:

  • RORγt binding to chromatinized DNA promotes coregulator recruitment and chromatin decompaction.
  • This study provides a mechanistic understanding of RORγt function within the chromatin environment.
  • Findings offer insights into adaptive immunity regulation by RORγt.