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Biomolecular Recognition of Methylated Histones

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The DNA, RNA, and Histone Methylomes

Part of the book series: RNA Technologies ((RNATECHN))

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Abstract

Lysine and arginine methylations are among the most abundant posttranslational modifications found on histone proteins. The recognition of methylated lysine and arginine residues by epigenetic reader proteins provides an important molecular requirement for regulation of human genes. Recent structural and mechanistic studies importantly advanced our basic understanding of biomolecular recognition of methylated histones by diverse classes of epigenetic readers. In this chapter, we describe chemical biological studies on the recognition of methylated histones by the aromatic cage-containing reader proteins.

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Acknowledgement

We thank the European Research Council for financial support (ERC Starting Grant to J.M., ChemEpigen-715691).

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Authors and Affiliations

  1. Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Odense, Denmark

    Miriam R. B. Porzberg & Jasmin Mecinović

  2. Institute for Molecules and Materials, Radboud University, Nijmegen, The Netherlands

    Bas J. G. E. Pieters & Jasmin Mecinović

Authors
  1. Miriam R. B. Porzberg
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  2. Bas J. G. E. Pieters
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  3. Jasmin Mecinović
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Corresponding author

Correspondence to Jasmin Mecinović .

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Editors and Affiliations

  1. Nanobiomedical Center, Adam Mickiewicz University, Poznań, Poland

    Stefan Jurga

  2. Nanobiomedical Center, Adam Mickiewicz University, Poznań, Poland

    Jan Barciszewski

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Porzberg, M.R.B., Pieters, B.J.G.E., Mecinović, J. (2019). Biomolecular Recognition of Methylated Histones. In: Jurga, S., Barciszewski, J. (eds) The DNA, RNA, and Histone Methylomes. RNA Technologies. Springer, Cham. https://doi.org/10.1007/978-3-030-14792-1_17

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