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O-GlcNAc transferase associates with the MCM2-7 complex and its silencing destabilizes MCM-MCM interactions

Maïté Leturcq1, Marlène Mortuaire1, Stéphan Hardivillé1

  • 1Univ. Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, 59000, Lille, France.

Cellular and Molecular Life Sciences : CMLS
|August 3, 2018
PubMed

Insights

O-GlcNAcylation regulates the MCM2-7 complex, crucial for DNA replication. This study reveals O-GlcNAc transferase (OGT) interacts with MCM proteins, affecting their chromatin binding and complex stability.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Protein O-GlcNAcylation, regulated by OGT and OGA, is vital for cell cycle progression.
  • The MCM2-7 complex, essential for DNA replication initiation, comprises MCM2, MCM3, MCM6, and MCM7 subunits.
  • Previous work identified O-GlcNAcylation of specific MCM subunits.

Purpose of the Study:

  • To investigate the role of O-GlcNAcylation in the regulation of the MCM2-7 complex.
  • To identify interactions between OGT and MCM subunits.
  • To determine how O-GlcNAcylation affects MCM protein chromatin binding and complex stability.

Main Methods:

  • Analysis of O-GlcNAcylation in synchronized human cells.
  • Co-immunoprecipitation to identify protein interactions.
  • Western blotting to assess protein levels and chromatin binding.
  • OGT knockdown and OGA inhibition experiments.

Main Results:

  • All six MCM2-7 subunits are O-GlcNAcylated, primarily in the chromatin-bound fraction.
  • OGT stably interacts with several MCM subunits.
  • OGT depletion reduces chromatin binding of MCM2, MCM6, and MCM7.
  • OGT depletion or OGA inhibition destabilizes MCM/MCM interactions within the chromatin-enriched fraction.

Conclusions:

  • O-GlcNAcylation, via OGT, is a novel regulator of the MCM2-7 complex.
  • O-GlcNAcylation homeostasis influences MCM complex function by modulating chromatin loading and subunit interactions.
Keywords:
Cell cycleChromatinDNA replicationO-GlcNAcylationPost-translational modificationPre-replicative complex

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