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Phosphorylation event changes the RNA binding mode of EZH2 disordered segment.

Beáta Szabó1, András Micsonai2,3, József Kardos3,4

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|December 23, 2025
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Summary

Polycomb repressive complex 2 (PRC2) interacts with long non-coding RNAs (lncRNAs) like HOTAIR. Phosphorylation of the EZH2 subunit

Keywords:
EZH2HOTAIRPRC2circular dichroismintrinsically disordered proteinlncRNAmicroscale thermophoresisprotein–RNA interaction

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • RNA Biology

Background:

  • Polycomb repressive complex 2 (PRC2) is crucial for gene silencing in development and differentiation.
  • Long non-coding RNAs (lncRNAs), such as HOTAIR, interact with PRC2, influencing its function and localization.
  • The EZH2 subunit of PRC2 possesses RNA-binding surfaces, with one located in a disordered loop region.

Purpose of the Study:

  • To elucidate the molecular mechanisms of RNA recognition by the disordered loop of EZH2.
  • To investigate the impact of phosphorylation on the interaction between the EZH2 loop and lncRNAs.

Main Methods:

  • Expression and purification of the disordered loop region of EZH2.
  • In vitro binding assays using various RNA constructs, including segments of HOTAIR.
  • Characterization of the structural changes upon RNA binding and phosphorylation using biophysical techniques.

Main Results:

  • The EZH2 loop binds to different RNA species with varying affinities and limited sequence specificity.
  • Phosphorylation did not significantly alter binding affinity but modulated the interaction's structural context.
  • A phosphomimetic EZH2 loop mutant could unfold double-stranded RNA regions upon binding, unlike the unphosphorylated form.

Conclusions:

  • The study provides molecular insights into how disordered regions of EZH2 recognize and interact with lncRNAs.
  • Phosphorylation of the EZH2 loop plays a regulatory role by altering the structural dynamics of RNA interaction.
  • These findings clarify the mechanism of RNA binding by EZH2 and the functional significance of its phosphorylation.