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Protein lysine methyltransferase G9a acts on non-histone targets

Nature Chemical Biology volume 4, pages 344–346 (2008)Cite this article

Abstract

By methylation of peptide arrays, we determined the specificity profile of the protein methyltransferase G9a. We show that it mostly recognizes an Arg-Lys sequence and that its activity is inhibited by methylation of the arginine residue. Using the specificity profile, we identified new non-histone protein targets of G9a, including CDYL1, WIZ, ACINUS and G9a (automethylation), as well as peptides derived from CSB. We demonstrate potential downstream signaling pathways for methylation of non-histone proteins.

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Figure 1: Specificity analysis of human G9a SET domain.
Figure 2: Methylation of new G9a targets.
Figure 3: HP1β binding to modified and unmodified peptides analyzed using peptide arrays.

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References

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

    Article  CAS  Google Scholar 

  2. Rea, S. et al. Nature 406, 593–599 (2000).

    Article  CAS  Google Scholar 

  3. Cheng, X., Collins, R.E. & Zhang, X. Annu. Rev. Biophys. Biomol. Struct. 34, 267–294 (2005).

    Article  CAS  Google Scholar 

  4. Tachibana, M. et al. Genes Dev. 16, 1779–1791 (2002).

    Article  CAS  Google Scholar 

  5. Xin, Z. et al. J. Biol. Chem. 278, 14996–15000 (2003).

    Article  CAS  Google Scholar 

  6. Ikegami, K. et al. Genes Cells 12, 1–11 (2007).

    Article  CAS  Google Scholar 

  7. Tachibana, M. et al. Genes Dev. 19, 815–826 (2005).

    Article  CAS  Google Scholar 

  8. Collins, R.E. et al. J. Biol. Chem. 280, 5563–5570 (2005).

    Article  CAS  Google Scholar 

  9. Patnaik, D. et al. J. Biol. Chem. 279, 53248–53258 (2004).

    Article  CAS  Google Scholar 

  10. Tachibana, M., Sugimoto, K., Fukushima, T. & Shinkai, Y. J. Biol. Chem. 276, 25309–25317 (2001).

    Article  CAS  Google Scholar 

  11. Rathert, P., Zhang, X., Freund, C., Cheng, X. & Jeltsch, A. Chem. Biol. 15, 5–11 (2008).

    Article  CAS  Google Scholar 

  12. Chin, H.G. et al. Biochemistry 44, 12998–13006 (2005).

    Article  CAS  Google Scholar 

  13. Dacwag, C.S., Ohkawa, Y., Pal, S., Sif, S. & Imbalzano, A.N. Mol. Cell. Biol. 27, 384–394 (2007).

    Article  CAS  Google Scholar 

  14. Kirmizis, A. et al. Nature 449, 928–932 (2007).

    Article  CAS  Google Scholar 

  15. Guccione, E. et al. Nature 449, 933–937 (2007).

    Article  CAS  Google Scholar 

  16. Sampath, S.C. et al. Mol. Cell 27, 596–608 (2007).

    Article  CAS  Google Scholar 

  17. Jacobs, S.A. & Khorasanizadeh, S. Science 295, 2080–2083 (2002).

    Article  CAS  Google Scholar 

  18. Frank, R. J. Immunol. Methods 267, 13–26 (2002).

    Article  CAS  Google Scholar 

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Acknowledgements

The US National Institutes of Health (GM068680) and the Bundesministerium für Bildung und Forschung Biofuture program have supported this work. We thank M.T. Bedford (University of Texas M.D. Anderson Cancer Center) for the GST-HP1β expression construct and M. Yoshida (RIKEN) for technical advice on anti-pan methyllysine antibodies. Technical assistance by M. Schwerdtfeger (Jacobs University Bremen) is gratefully acknowledged.

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Authors and Affiliations

  1. Biochemistry Laboratory, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, Bremen, 28759, Germany

    Philipp Rathert, Arunkumar Dhayalan, Raluca Tamas, Renata Jurkowska & Albert Jeltsch

  2. Research Center for Infectious Diseases, Institute for Virus Research and Graduate School of Biostudies, Kyoto University, 53 Shogoin, Kawara-cho, Sakyo-ku, Kyoto, 606-8507, Kyoto, Japan

    Marie Murakami & Yoichi Shinkai

  3. Department of Biochemistry, Emory University School of Medicine, 1510 Clifton Road, Atlanta, 30322, Georgia, USA

    Xing Zhang & Xiaodong Cheng

  4. Biochemistry and Cell Biology Program, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, Bremen, 28759, Germany

    Raluca Tamas

  5. R&D Division, Advanced Life Science Institute Inc., 2-10-23, Maruyamadai, Wako, 351-0112, Saitama, Japan

    Yasuhiko Komatsu

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  1. Philipp Rathert
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Correspondence to Albert Jeltsch.

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Supplementary Text and Figures

Supplementary Figures 1–4, Supplementary Table 1, Supplementary Discussion and Supplementary Methods (PDF 421 kb)

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Rathert, P., Dhayalan, A., Murakami, M. et al. Protein lysine methyltransferase G9a acts on non-histone targets. Nat Chem Biol 4, 344–346 (2008). https://doi.org/10.1038/nchembio.88

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