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A Switch for Transcriptional Activation and Repression: Histone Arginine Methylation

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The DNA, RNA, and Histone Methylomes

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

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Abstract

Histones can be methylated on both lysine (K) and arginine (R) residues. Histone arginine methylation is a prevalent post-translational modification catalyzed by protein arginine methyltransferases (PRMTs). As an epigenetic modification, histone arginine methylation is associated with signal transduction, cell differentiation, cellular metabolism, tissue homeostasis, immune and inflammatory responses etc. Methylation at arginine residues alters the properties of the nucleosome to regulate gene transcription and the interaction between nucleosome and other regulatory proteins. Histone arginine methylation results in either transcriptional repression or activation. This review focuses on the biochemistry, regulatory mechanism, and the functional significance of histone arginine methylation.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine, Shanghai, P. R. China

    Tian-Shi Wang & Jin-Ke Cheng

  2. Fudan University Shanghai Cancer Center, Cancer Institute, Fudan University Cancer Hospital, and Cancer Metabolism Laboratory, Institutes of Biomedical Sciences, Fudan University, Shanghai, P. R. China

    Qun-Ying Lei & Yi-Ping Wang

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  1. Tian-Shi Wang
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  2. Jin-Ke Cheng
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Correspondence to Yi-Ping Wang .

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

    Stefan Jurga

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

    Jan Barciszewski

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Wang, TS., Cheng, JK., Lei, QY., Wang, YP. (2019). A Switch for Transcriptional Activation and Repression: Histone Arginine Methylation. 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_21

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