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Related Concept Videos

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Cortical Actin Flow in T Cells Quantified by Spatio-temporal Image Correlation Spectroscopy of Structured Illumination Microscopy Data
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Structure and functional interactions of INO80 actin/Arp module.

Xuan Zhang1, Xuejuan Wang1, Zhihui Zhang1

  • 1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science & Technology of China, Hefei, China.

Journal of Molecular Cell Biology
|November 3, 2018
PubMed
Summary

Nuclear actin and actin-related proteins (Arps) are key to the INO80 chromatin remodeler. This study reveals how the INO80 actin/Arp module binds nucleosomes, acting as a conformational switch for chromatin remodeling.

Keywords:
INO80actin/Arp–Nuc207 assemblymodular architecturenuclear actin/Arp module

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Chromatin Biology

Background:

  • Nuclear actin and actin-related proteins (Arps) are integral components of chromatin remodeling complexes.
  • The INO80 complex, a conserved chromatin remodeler, utilizes actin/Arp subunits, but its precise molecular mechanisms remain unclear.

Purpose of the Study:

  • To elucidate the molecular mechanisms of nuclear actin function within the INO80 chromatin-remodeling complex.
  • To determine the structure and nucleosome-binding interactions of the INO80 actin/Arp module.

Main Methods:

  • Improved cryo-electron microscopy (cryo-EM) for structural determination.
  • 3D reconstruction of the INO80 actin/Arp module and its interaction with nucleosomes.
  • Subunit deletion analysis and crosslinking-mass spectrometry for architectural definition.

Main Results:

  • An improved cryo-EM structure of the yeast INO80 complex was obtained.
  • The first 3D reconstruction of the INO80 actin/Arp module revealed its modular architecture.
  • Nucleosome binding initiates at the Arp8 subunit, inducing conformational changes that enhance contacts and facilitate engagement with the INO80 ATPase domain.

Conclusions:

  • The conserved nuclear actin/Arp module functions as a conformational switch for the INO80 complex.
  • This mechanism is crucial for regulating nucleosome binding and subsequent chromatin remodeling activities.
  • The findings provide critical molecular insights into the controversial roles of nuclear actin.