MCM2 binding to histones H3–H4 and ASF1 supports a tetramer-to-dimer model for histone inheritance at the replication fork

@article{Clment2015MCM2BT,
  title={MCM2 binding to histones H3–H4 and ASF1 supports a tetramer-to-dimer model for histone inheritance at the replication fork},
  author={Camille Cl{\'e}ment and Genevi{\`e}ve Almouzni},
  journal={Nature Structural &Molecular Biology},
  year={2015},
  volume={22},
  pages={587-589}
}
587 helicase complex. This suggests that the interaction of MCM2 with histones involving a tetramer-to-dimer transition is important for the proper function of the replication machinery. The work provides a molecular framework coordinating histone H3–H4 recycling with replication-fork progression. Finally, after finding that MCM2 binds all H3 variants (H3.1, H3.2, H3.3 and CENP-A), the authors proposed that this mechanism to handle histones probably applies throughout the entire genome. MCM2… CONTINUE READING
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n e w s a n d v i e w s np g © 2 01 5 N at ur e A m

  • K. Shibahara, B. Stillman
  • Cell
  • 1999

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