Histone arginine methylation and its dynamic regulation

10.2741/1802 ◽  
2006 ◽  
Vol 11 (1) ◽  
pp. 344 ◽  
Author(s):  
Joanna Wysocka
Keyword(s):  
Arginine Methylation ◽  
Dynamic Regulation ◽  
Histone Arginine Methylation

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

2009 ◽  
Vol 29 (2) ◽  
pp. 131-141 ◽  
Author(s):  
Michael Litt ◽  
Yi Qiu ◽  
Suming Huang
Keyword(s):  
Transcriptional Repression ◽  
Regulation Of Gene Expression ◽  
Arginine Methylation ◽  
Nuclear Proteins ◽  
Lysine Methylation ◽  
Histone Tails ◽  
Dynamic Regulation ◽  
Chromatin Dynamics ◽  
Arginine Residues ◽  
Histone Arginine Methylation

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.

scholarly journals PADI4 acts as a coactivator of Tal1 by counteracting repressive histone arginine methylation

2014 ◽  
Vol 5 (1) ◽  
Author(s):  
Stephan Kolodziej ◽  
Olga N. Kuvardina ◽  
Thomas Oellerich ◽  
Julia Herglotz ◽  
Ingo Backert ◽  
...  
Keyword(s):  
Arginine Methylation ◽  
Histone Arginine Methylation

scholarly journals Histone arginine methylation

FEBS Letters ◽  
2010 ◽  
Vol 585 (13) ◽  
pp. 2024-2031 ◽  
Author(s):  
Alessandra Di Lorenzo ◽  
Mark T. Bedford
Keyword(s):  
Arginine Methylation ◽  
Histone Arginine Methylation

scholarly journals Histone Arginine Methylation by PRMT7 Controls Germinal Center Formation via Regulating Bcl6 Transcription

2015 ◽  
Vol 195 (4) ◽  
pp. 1538-1547 ◽  
Author(s):  
Zhengzhou Ying ◽  
Mei Mei ◽  
Peizhun Zhang ◽  
Chunyi Liu ◽  
Huacheng He ◽  
...  
Keyword(s):  
Germinal Center ◽  
Arginine Methylation ◽  
Histone Arginine Methylation ◽  
Germinal Center Formation

scholarly journals Histone Arginine Methylation-Mediated Epigenetic Regulation of Discoidin Domain Receptor 2 Controls the Senescence of Human Bone Marrow Mesenchymal Stem Cells

2019 ◽  
Vol 2019 ◽  
pp. 1-14 ◽  
Author(s):  
Zhenyu Xu ◽  
Wenming Wu ◽  
Fang Shen ◽  
Yue Yu ◽  
Yue Wang ◽  
...  
Keyword(s):  
Stem Cells ◽  
Bone Marrow ◽  
Mesenchymal Stem Cells ◽  
Cellular Senescence ◽  
Arginine Methylation ◽  
Early Passage ◽  
Marrow Mesenchymal Stem Cells ◽  
Discoidin Domain Receptor 2 ◽  
Histone Arginine Methylation

The application of human bone marrow mesenchymal stem cells (hBM-MSCs) in cell-based clinical therapies is hindered by the limited number of cells remaining after the initial isolation process and by cellular senescence following in vitro expansion. Understanding the process of in vitro senescence in hBM-MSCs would enable the development of strategies to maintain their vitality after cell culture. Herein, we compared the gene expression profiles of human embryonic stem cells and human BM-MSCs from donors of different ages. We first found that the expression of discoidin domain receptor 2 (DDR2) in adult donor-derived hBM-MSCs was lower than it was in the young donor-derived hBM-MSCs. Moreover, in vitro cultured late-passage hBM-MSCs showed significant downregulation of DDR2 compared to their early-passage counterparts, and siRNA inhibition of DDR2 expression recapitulated features of senescence in early-passage hBM-MSCs. Further, we found through knockdown and overexpression approaches that coactivator-associated arginine methyltransferase 1 (CARM1) regulated the expression level of DDR2 and the senescence of hBM-MSCs. Finally, chromatin immunoprecipitation analysis confirmed direct binding of CARM1 to the DDR2 promoter region with a high level of H3R17 methylation in early-passage hBM-MSCs, and inhibition of CARM1-mediated histone arginine methylation decreased DDR2 expression and led to cellular senescence. Taken together, our findings suggest that DDR2 plays a major role in regulating the in vitro senescence of hBM-MSCs and that CARM1-mediated histone H3 methylation might be the upstream regulatory mechanism controlling this function of DDR2.

scholarly journals KSHV ORF59 and PAN RNA Recruit Histone Demethylases to the Viral Chromatin during Lytic Reactivation

Viruses ◽  
2020 ◽  
Vol 12 (4) ◽  
pp. 420
Author(s):  
Kayla Hiura ◽  
Roxanne Strahan ◽  
Timsy Uppal ◽  
Brian Prince ◽  
Cyprian C. Rossetto ◽  
...  
Keyword(s):  
Viral Genome ◽  
Arginine Methylation ◽  
Histone Demethylases ◽  
Methyl Transferase ◽  
Lytic Reactivation ◽  
Viral Genes ◽  
Nuclear Rna ◽  
Processivity Factor ◽  
Epigenetic Gene Regulation ◽  
Histone Arginine Methylation

Kaposi’s sarcoma-associated herpesvirus (KSHV) causes multiple malignancies in immunocompromised individuals. KSHV primarily establishes a lifelong latency in infected humans during which only a subset of viral genes is expressed while most of the viral genome remains transcriptionally silent with condensed chromatin. However, during the lytic phase, the viral genome undergoes dramatic changes in chromatin landscape leading to a transcriptionally active state with the expression of most of the viral genes and production of progeny virions. Multiple cellular and viral factors influence the epigenetic gene regulation and transitioning of virus from latency to the lytic state. We have earlier shown that KSHV ORF59, viral processivity factor, binds to a protein arginine methyl transferase 5 (PRMT5) to alter the histone arginine methylation during reactivation. Additionally, ORF59 has been shown to interact with most abundantly expressed KSHV long noncoding polyadenylated nuclear RNA (PAN RNA), which associates with the viral epigenome during reactivation. Interestingly, PAN RNA interacts with UTX and JMJD3, cellular H3K27me3 demethylases, and removes the repressive marks on the chromatin. In this study, we report that the recruitment of histone demethylases to the viral chromatin is facilitated by the expression of ORF59 protein and PAN RNA. Using biochemical and localization assays including co-immunoprecipitation and immunofluorescence, we demonstate ORF59 localizes with UTX and JMJD3. Our results confirm that PAN RNA enhances the interaction of ORF59 with the chromatin modifying enzymes UTX and JMJD3.

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