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ATRX ADD domain is a versatile module for recognizing macroH2A, H3, and beyond.

Shukun Yan1, Xiaoman Wang1, Kexue Ge1

  • 1Key Laboratory of Epigenetic Regulation and Intervention, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences; University of Chinese Academy of Sciences, Shanghai 200031, China.

Acta Biochimica Et Biophysica Sinica
|May 30, 2025
PubMed
Summary

Alpha Thalassemia/Mental developmental retardation, X-linked (ATRX) protein interacts with histone variant macroH2A via its ADD domain. This interaction is key for epigenetic regulation and genome stability, revealing new insights into ATR-X syndrome and cancer pathogenesis.

Keywords:
ADD domainATRXMacroH2ANURD complexchromatin remodelinghistone variant

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Area of Science:

  • Epigenetics and Molecular Biology
  • Chromatin Biology
  • Cancer Research

Background:

  • Alpha Thalassemia/Mental developmental retardation, X-linked (ATRX) is a critical regulator of heterochromatin, frequently mutated in ATR-X syndrome and various cancers.
  • ATRX interacts with the histone variant macroH2A, forming a complex vital for transcription regulation and genome stability.
  • The precise molecular mechanism of the ATRX-macroH2A interaction is not well understood.

Purpose of the Study:

  • To elucidate the molecular mechanism underlying the interaction between ATRX and macroH2A.
  • To investigate the binding specificity and interface of the ATRX ADD domain with macroH2A.
  • To identify other proteins interacting with the ATRX ADD domain.

Main Methods:

  • X-ray crystallography and structural analysis of ATRX ADD domain and macroH2A.
  • Site-directed mutagenesis to probe binding interfaces.
  • Affinity purification coupled with mass spectrometry (AP-MS) to identify interacting proteins.

Main Results:

  • The ADD domain of ATRX specifically binds the histone-fold domain of macroH2A, not canonical H2A.
  • A D/E-rich loop in ATRX ADD and the L12 loop of macroH2A mediate this specific binding.
  • ATRX ADD utilizes a conserved interface for binding both macroH2A and histone H3, suggesting competitive binding.
  • NuRD components and CDH4 were identified as potential ATRX ADD-associating proteins.

Conclusions:

  • The study reveals the molecular basis for ATRX-macroH2A interaction, highlighting the role of specific loops and interfaces.
  • ATRX ADD domain exhibits versatility in recognizing diverse chromatin regulators, including histones and NuRD components.
  • These findings offer crucial insights into ATRX's multifaceted roles in epigenetic regulation, genome stability, and disease pathogenesis.