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Biochim Biophys Acta. 2016 Aug;1863(8):2093-103. doi: 10.1016/j.bbamcr.2016.05.009. Epub 2016 May 13.

Methylation of arginine by PRMT1 regulates Nrf2 transcriptional activity during the antioxidative response.

Author information

1
The Institute of Genetics and Cytology, Northeast Normal University, Changchun 130024, China.
2
The Key Laboratory of Molecular Epigenetics of the Ministry of Education, Northeast Normal University, Changchun 130021, China.
3
The Institute of Genetics and Cytology, Northeast Normal University, Changchun 130024, China. Electronic address: zhangy288@nenu.edu.cn.
4
The Key Laboratory of Molecular Epigenetics of the Ministry of Education, Northeast Normal University, Changchun 130021, China. Electronic address: luj809@nenu.edu.cn.

Abstract

The cap 'n' collar (CNC) family of transcription factors play important roles in resistance of oxidative and electrophilic stresses. Among the CNC family members, NF-E2-related factor 2 (Nrf2) is critical for regulating the antioxidant and phase II enzymes through antioxidant response element (ARE)-mediated transactivation. The activity of Nrf2 is controlled by a variety of post-translational modifications, including phosphorylation, ubiquitination, acetylation and sumoylation. Here we demonstrate that the arginine methyltransferase-1 (PRMT1) methylates Nrf2 protein at a single residue of arginine 437, both in vitro and in vivo. Using the heme oxygenase-1 (HO-1) as a model of phase II enzyme gene, we found that methylation of Nrf2 by PRMT1 led to a moderate increase of its DNA-binding activity and transactivation, which subsequently protected cells against the tBHP-induced glutathione depletion and cell death. Collectively, our results define a novel modification of Nrf2, which operates as a fine-tuning mechanism for the transcriptional activity of Nrf2 under the oxidative stress.

KEYWORDS:

HO-1; Methylation of arginine; Nrf2; Oxidative stress; PRMT1

PMID:
27183873
DOI:
10.1016/j.bbamcr.2016.05.009
[Indexed for MEDLINE]
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