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

Nature Structural & Molecular Biology volume 22, pages 587–589 (2015)Cite this article

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MCM2, a component of the replicative helicase, can bind histones H3–H4 in both tetrameric and dimeric form, depending on the presence of the histone chaperone ASF1. A structural analysis of the complexes now sheds light on key domains in the MCM2 protein that prove important for cell proliferation.

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Figure 1: Dynamics of histones at the replication fork.
Figure 2: MCM2 binding to both histones H3–H4 and ASF1 supports a tetramer-to-dimer model in the recycling of parental H3–H4 at the replication fork.

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References

  1. Probst, A.V., Dunleavy, E. & Almouzni, G. Nat. Rev. Mol. Cell Biol. 10, 192–206 (2009).

    Article  CAS  PubMed  Google Scholar 

  2. Huang, H. et al. Nat. Struct. Mol. Biol. 22, 618–626 (2015).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  3. Richet, N. et al. Nucleic Acids Res. 43, 1905–1917 (2015).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  4. Mousson, F. et al. Proc. Natl. Acad. Sci. USA 102, 5975–5980 (2005).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  5. English, C.M. et al. Cell 127, 495–508 (2006).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  6. Natsume, R. et al. Nature 446, 338–341 (2007).

    Article  CAS  PubMed  Google Scholar 

  7. Ishimi, Y. et al. J. Biol. Chem. 271, 24115–24122 (1996).

    Article  CAS  PubMed  Google Scholar 

  8. Groth, A. et al. Mol. Cell 17, 301–311 (2005).

    Article  CAS  PubMed  Google Scholar 

  9. Groth, A. et al. Science 318, 1928–1931 (2007).

    Article  CAS  PubMed  Google Scholar 

  10. Loyola, A. et al. Mol. Cell 24, 309–316 (2006).

    Article  CAS  PubMed  Google Scholar 

  11. Jasencakova, Z. et al. Mol. Cell 37, 736–743 (2010).

    Article  CAS  PubMed  Google Scholar 

  12. Xu, M. et al. Science 328, 94–98 (2010).

    Article  CAS  PubMed  Google Scholar 

  13. Tang, Y. et al. Nat. Struct. Mol. Biol. 13, 921–929 (2006).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  14. Abascal, F. et al. Mol. Biol. Evol. 30, 1853–1866 (2013).

    Article  CAS  PubMed  Google Scholar 

  15. Ricketts, D.M. et al. Nat. Commun. 6, 7711 (2015).

    Article  PubMed  Google Scholar 

  16. Quivy, J.P., Grandi, P. & Almouzni, G. EMBO J. 20, 2015–2027 (2001).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  17. Shibahara, K. & Stillman, B. Cell 96, 575–585 (1999).

    Article  CAS  PubMed  Google Scholar 

  18. Gérard, A. et al. EMBO Rep. 7, 817–823 (2006).

    PubMed  PubMed Central  Google Scholar 

  19. Cook, A.J. et al. Mol. Cell 44, 918–927 (2011).

    CAS  PubMed  Google Scholar 

  20. Lacoste, N. et al. Mol. Cell 53, 631–644 (2014).

    Article  CAS  PubMed  Google Scholar 

  21. Arimura, Y. et al. Sci. Rep. 4, 7115 (2014).

    Article  PubMed  PubMed Central  Google Scholar 

  22. Nakano, S., Stillman, B. & Horvitz, H.R. Cell 147, 1525–1536 (2011).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  23. Chen, S. et al. Genes Dev. 29, 1326–1340 (2015).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  24. Corpet, A. & Almouzni, G. Trends Cell Biol. 19, 29–41 (2009).

    Article  CAS  PubMed  Google Scholar 

  25. Luger, K. et al. Nature 389, 251–260 (1997).

    Article  CAS  PubMed  Google Scholar 

Download references

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Authors and Affiliations

  1. Camille Clément and Geneviève Almouzni are at the Institut Curie, Paris Sciences et Lettres Research University, “Nuclear Dynamics,” UMR3664, CNRS, Université Pierre et Marie Curie, Paris, France.,

    Camille Clément & Geneviève Almouzni

  2. Geneviève Almouzni is Director of the Research Center, Institut Curie, and coordinator of the Network of Excellence EpiGeneSys.,

    Geneviève Almouzni

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  1. Camille Clément
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  2. Geneviève Almouzni
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Correspondence to Geneviève Almouzni.

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Clément, C., Almouzni, G. MCM2 binding to histones H3–H4 and ASF1 supports a tetramer-to-dimer model for histone inheritance at the replication fork. Nat Struct Mol Biol 22, 587–589 (2015). https://doi.org/10.1038/nsmb.3067

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