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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
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Polycomb repressive complex 2 in an autoinhibited state.

Matthew Bratkowski1, Xin Yang1, Xin Liu2

  • 1From the Cecil H. and Ida Green Center for Reproductive Biology Sciences and Division of Basic Research, Department of Obstetrics and Gynecology, Department of Biophysics, UT Southwestern Medical Center, Dallas, Texas 75390.

The Journal of Biological Chemistry
|June 14, 2017
PubMed
Summary
This summary is machine-generated.

Polycomb repressive complex 2 (PRC2) can be autoinhibited, a novel state revealed by crystal structure. This autoinhibition is reversed by cofactor binding, vastly activating the enzyme for epigenetic gene silencing.

Keywords:
crystal structureenzymeepigeneticshistone methylationpolycomb

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Area of Science:

  • Epigenetics
  • Structural Biology
  • Enzymology

Background:

  • Polycomb-group proteins regulate fundamental biological processes via epigenetic gene silencing.
  • Polycomb repressive complex 2 (PRC2) catalyzes histone H3 lysine 27 (H3K27) methylation, forming H3K27me3 marks.
  • PRC2 is highly conserved across species, indicating fundamental roles in gene regulation.

Purpose of the Study:

  • To determine the crystal structure of an autoinhibited state of PRC2.
  • To investigate the role of cofactor binding in regulating PRC2 activity.
  • To understand the structural basis of PRC2 regulation and activation.

Main Methods:

  • X-ray crystallography to determine the structure of apo-PRC2.
  • Biochemical assays to study cofactor binding.
  • Enzyme kinetics to measure PRC2 activity.

Main Results:

  • The crystal structure of fungal Chaetomium thermophilum apo-PRC2 revealed a novel autoinhibited conformation.
  • Binding of S-adenosylmethionine (SAM) cofactor mitigates the autoinhibited state.
  • Disrupting autoinhibition significantly increases PRC2 enzyme activity.

Conclusions:

  • Autoinhibition represents a novel regulatory mechanism for PRC2.
  • This regulatory mechanism allows control of PRC2 activity in response to cellular signals.
  • The autoinhibited state provides a platform for PRC2 activation, influencing epigenetic gene silencing.