PARAQUAT TOLERANCE3 Is an E3 Ligase That Switches off Activated Oxidative Response by Targeting Histone-Modifying PROTEIN METHYLTRANSFERASE4b

Oxidative stress is unavoidable for aerobic organisms. when abiotic and biotic stresses are encountered,oxidative damage could occur in cells. to avoid this damage,defense mechanisms must be timely and efficiently modulated. while the response to oxidative stress has been extensively studied in plants,little is known about how the activated response is switched off when oxidative stress is diminished. by studying arabidopsis mutant paraquat tolerance3,we identified the genetic locus paraquat tolerance3 (pqt3) as a major negative regulator of oxidative stress tolerance. pqt3,encoding an e3 ubiquitin ligase,is rapidly down-regulated by oxidative stress. pqt3 has e3 ubiquitin ligase activity in ubiquitination assay. subsequently,we identified prmt4b as a pqt3-interacting protein. by histone methylation,prmt4b upregulates the expression of apx1 and gpx1,encoding two key enzymes against oxidative stress. on the other hand,prmt4b is recognized by pqt3 for targeted degradation via 26s proteasome. therefore,we have identified pqt3 as an e3 ligase that acts as a negative regulator of activated response to oxidative stress and found that histone modification by prmt4b at apx1 and gpx1 loci plays an important role in oxidative stress tolerance. © 2016 luo et al.