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MBD5 and MBD6 interact with the human PR-DUB complex through their methyl-CpG-binding domain

H Irem Baymaz1, Alexandra Fournier, Sophie Laget

  • 1Molecular Cancer Research, Cancer Genomics, University Medical Center Utrecht, Utrecht, The Netherlands.

Proteomics
|March 18, 2014
PubMed

Insights

Methyl-CpG-binding domain (MBD) proteins MBD5 and MBD6 interact with the PR-DUB complex. MBD6 is recruited to DNA damage sites, suggesting distinct roles for these MBD proteins.

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Protein Interactions

Background:

  • Methyl-CpG-binding domain (MBD) proteins MBD5 and MBD6 are poorly understood.
  • Previous studies did not demonstrate MBD5/MBD6 MBD binding to methylated DNA.

Purpose of the Study:

  • To investigate the function and interactions of MBD5 and MBD6.
  • To elucidate the role of the MBD domain in MBD5/MBD6 interactions.

Main Methods:

  • Protein interaction assays.
  • Mammalian PR-DUB Polycomb complex analysis.
  • Chromatin immunoprecipitation (ChIP).

Main Results:

  • MBD5 and MBD6 bind the PR-DUB complex mutually exclusively.
  • The MBD of MBD5 and MBD6 is essential and sufficient for PR-DUB interaction.
  • MBD6 and FOXK2/PR-DUB share genomic targets.
  • MBD6, unlike MBD5, is recruited to DNA damage sites independently of PR-DUB.

Conclusions:

  • MBD5 and MBD6 share a function via PR-DUB interaction.
  • MBD6 has a specific role in DNA damage response.
Keywords:
Cell biologyChromatinProtein-protein interactions

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