Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10801734 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2016 | 11 Pages |
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
Heme oxygenase-1Txnrd1PRMT1tBHPGCLMCARM1Coactivator-associated arginine methyltransferase 1NQO1HO-1Nrf2DMEMPEIDulbecco's modified Eagle's mediumt-Butyl hydroperoxideThioredoxin reductase 1Oxidative stressNF-E2-related factor 2antioxidant response elementAREpolyethyleneimineglutamate-cysteine ligase modifier subunit
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Authors
Xin Liu, Hongyuan Li, Lingxia Liu, Yang Lu, Yanyan Gao, Pengyu Geng, Xiaoxue Li, Baiqu Huang, Yu Zhang, Jun Lu,