Histone arginine methylations: their roles in chromatin dynamics and transcriptional regulation

Author:

Litt Michael1,Qiu Yi23,Huang Suming345

Affiliation:

1. Medical Education Center, Ball State University, Muncie, IN 47302, U.S.A.

2. Department of Anatomy and Cell Biology, University of Florida College of Medicine, Gainesville, FL 32611, U.S.A.

3. Shands Cancer Center, University of Florida College of Medicine, Gainesville, FL 32611, U.S.A.

4. Department of Biochemistry and Molecular Biology, University of Florida College of Medicine, Gainesville, FL 32611, U.S.A.

5. Genetics Institute, University of Florida College of Medicine, Gainesville, FL 32611, U.S.A.

Abstract

PRMTs (protein arginine N-methyltransferases) specifically modify the arginine residues of key cellular and nuclear proteins as well as histone substrates. Like lysine methylation, transcriptional repression or activation is dependent upon the site and type of arginine methylation on histone tails. Recent discoveries imply that histone arginine methylation is an important modulator of dynamic chromatin regulation and transcriptional controls. However, under the shadow of lysine methylation, the roles of histone arginine methylation have been under-explored. The present review focuses on the roles of histone arginine methylation in the regulation of gene expression, and the interplays between histone arginine methylation, histone acetylation, lysine methylation and chromatin remodelling factors. In addition, we discuss the dynamic regulation of arginine methylation by arginine demethylases, and how dysregulation of PRMTs and their activities are linked to human diseases such as cancer.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

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