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Targeting the JMJD2A histone lysine demethylase

Nature Structural & Molecular Biology volume 14, pages 682–684 (2007)Cite this article

Targeting of enzymes regulating chromatin organization to specific histone residues is a key element in the hugely complex system of epigenetic signaling that controls gene regulation and repair. Understanding of how targeting is achieved is still limited, but structures of the histone lysine demethylase JMJD2A in complex with substrate peptides now offer insight into its dual specificity.

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Figure 1: JMJD2A has dual specificity for both H3K9 and H3K36 target lysines, but despite differences in the adjacent sequence, both have a similar mode of binding.
Figure 2: Schematic representation of the different methyl-binding environments, showing how they influence substrate specificity.

Kim Caesar

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References

  1. Felsenfeld, G. & Groudine, M. Nature 421, 448–453 (2003).

    Article  Google Scholar 

  2. Jenuwein, T. & Allis, C.D. Science 293, 1074–1080 (2001).

    Article  CAS  Google Scholar 

  3. Kouzarides, T. Cell 128, 693–705 (2007).

    Article  CAS  Google Scholar 

  4. Berger, S.L. Nature 447, 407–412 (2007).

    Article  CAS  Google Scholar 

  5. Martin, C. & Zhang, Y. Nat. Rev. Mol. Cell Biol. 6, 838–849 (2005).

    Article  CAS  Google Scholar 

  6. Couture, J.F., Collazo, E., Ortiz-Tello, P.A., Brunzelle, J.S. & Trievel, R.C. Nat. Struct. Mol. Biol. 14, 689–695 (2007).

    Article  CAS  Google Scholar 

  7. Ng, S.S. et al. Nature 448, 87–91 (2007).

    Article  CAS  Google Scholar 

  8. Chen, Z. et al. Proc. Natl. Acad. Sci. USA 104, 10818–10823 (2007).

    Article  CAS  Google Scholar 

  9. Metzger, E. & Schule, R. Nat. Struct. Mol. Biol. 14, 252–254 (2007).

    Article  CAS  Google Scholar 

  10. Shi, Y. et al. Cell 119, 941–953 (2004).

    Article  CAS  Google Scholar 

  11. Tsukada, Y. et al. Nature 439, 811–816 (2006).

    Article  CAS  Google Scholar 

  12. Klose, R.J., Kallin, E.M. & Zhang, Y. Nat. Rev. Genet. 7, 715–727 (2006).

    Article  CAS  Google Scholar 

  13. Dillon, S.C., Zhang, X., Trievel, R.C. & Cheng, X. Genome Biol. 6, 227 (2005).

    Article  Google Scholar 

  14. Chen, Z. et al. Cell 125, 691–702 (2006).

    Article  CAS  Google Scholar 

  15. Whetstine, J.R. et al. Cell 125, 467–481 (2006).

    Article  CAS  Google Scholar 

  16. Forneris, F., Binda, C., Adamo, A., Battaglioli, E. & Mattevi, A. J. Biol. Chem. 282, 20070–20074 (2007).

    Article  CAS  Google Scholar 

Download references

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  1. Jon Wilson is in the Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK. jon.wilson@icr.ac.uk,

    Jon R Wilson

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Wilson, J. Targeting the JMJD2A histone lysine demethylase. Nat Struct Mol Biol 14, 682–684 (2007). https://doi.org/10.1038/nsmb0807-682

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