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Structural Insights into BAF47 and BAF155 Complex Formation.

Li Yan1, Si Xie1, Yongming Du1

  • 1School of Biomedical Sciences, The University of Hong Kong, Hong Kong SAR, China.

Journal of Molecular Biology
|April 26, 2017
PubMed
Summary
This summary is machine-generated.

Mammalian BAF complexes, crucial for gene regulation, involve interactions between BAF155 and BAF47. This study reveals the specific SWIRM/RPT1 domains mediating this interaction, distinct from other SWIRM domains.

Keywords:
BAF155BAF47RPT1SWIRMX-ray crystallography

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Mammalian BAF complexes are ATP-dependent chromatin remodelers essential for cellular processes.
  • BAF complexes are polymorphic, with up to 15 subunits from 29 genes.
  • BRG1/BRM, BAF47, and BAF155/BAF170 are core components of BAF complexes.

Purpose of the Study:

  • To elucidate the molecular interaction between BAF155 and BAF47.
  • To characterize the specific domains involved in the BAF155-BAF47 interaction.
  • To determine the structural basis of this interaction.

Main Methods:

  • X-ray crystallography to obtain high-resolution structures.
  • Site-directed mutagenesis to probe interaction interfaces.
  • Isothermal titration calorimetry and NMR titrations to confirm binding.

Main Results:

  • The SWIRM domain of BAF155 interacts with the Repeat 1 (RPT1) domain of BAF47.
  • The crystal structure of the SWIRM/RPT1 complex was determined.
  • Mutagenesis and biophysical methods confirmed the interaction interface.

Conclusions:

  • BAF155's SWIRM domain is a modular interaction module for BAF47.
  • This interaction is functionally distinct from other SWIRM domains known for DNA binding.