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Cooperative DNA looping by PRC2 complexes.

Xingcheng Lin1, Rachel Leicher2,3, Shixin Liu2

  • 1Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.

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|May 31, 2021
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Summary
This summary is machine-generated.

Polycomb repressive complex 2 (PRC2) binds and bends DNA, forming loops. Accessory proteins like AEBP2 regulate this interaction, potentially controlling where PRC2 acts in the genome.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Polycomb repressive complex 2 (PRC2) is crucial for gene silencing through chromatin modification.
  • Understanding PRC2's structure and DNA interactions is key to deciphering its regulatory mechanisms.

Purpose of the Study:

  • To characterize the full-length structure of PRC2.
  • To investigate PRC2-DNA interactions, including binding and DNA bending.
  • To elucidate the role of accessory proteins in PRC2-DNA complex formation.

Main Methods:

  • Homology modeling
  • Atomistic and coarse-grained molecular dynamics simulations
  • Single-molecule force spectroscopy
  • Free energy calculations with a novel protein-DNA force field

Main Results:

  • EZH2, a core PRC2 subunit, mediates primary DNA binding and induces DNA bending.
  • The SUZ12 subunit's C2 domain also contacts DNA.
  • PRC2 complexes bind DNA cooperatively, inducing DNA looping via allosteric communication.
  • AEBP2 regulates DNA looping by preventing C2 domain binding to DNA.

Conclusions:

  • PRC2 binding to DNA is structurally characterized, revealing EZH2's role in binding and bending.
  • PRC2-mediated DNA looping is confirmed, with AEBP2 acting as a key regulator.
  • Accessory proteins may control PRC2's genomic localization by modulating its DNA interactions.