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Highly disordered histone H1-DNA model complexes and their condensates.

Abigail L Turner1, Matthew Watson1, Oscar G Wilkins1

  • 1Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom.

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|October 11, 2018
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Summary

Histone H1's disordered tail (CH1) binds DNA and forms phase-separated droplets. Phosphorylation alters higher-order structures, revealing how posttranslational modifications regulate chromatin.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Disordered proteins are crucial for biological processes and often undergo posttranslational modifications.
  • The C-terminal tail of histone H1 (CH1) is highly disordered and involved in chromatin condensation, a process poorly understood.
  • CH1 phosphorylation varies with the cell cycle, correlating with chromatin condensation levels.

Purpose of the Study:

  • To develop a model system for analyzing CH1/DNA condensation.
  • To investigate the structural and biophysical properties of CH1/DNA complexes before and after condensation.
  • To understand the role of CH1 phosphorylation in regulating higher-order chromatin structure.

Main Methods:

  • Development of a model system to study CH1/DNA interactions.
  • Biophysical and structural analyses of CH1/DNA complexes.
  • Investigation of the effects of phosphorylation on condensate properties.

Main Results:

  • CH1 remains disordered upon DNA binding, even with nanomolar affinity.
  • CH1/DNA complexes form phase-separated droplets (coacervates) exhibiting higher-order assemblies.
  • Phosphorylation of CH1 significantly alters coacervate higher-order structure and reduces its partitioning, despite minimal local effects.

Conclusions:

  • Disordered proteins can bind DNA tightly without transitioning to an ordered state.
  • Posttranslational modifications can profoundly impact the higher-order structure of macromolecular assemblies like chromatin.
  • This study provides mechanistic insights into the regulation of chromatin and other assemblies by posttranslational modifications.