Exploring the effects of oxidation onPRMT1 activity

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Joan Hevel


Oxidative stress has been associated with the progression of many human diseases. It is well established that reactive oxygen species (ROS) are able to damage biomolecules, yet the molecular mechanisms of how oxidative stress contributes to human diseases remain largely elusive. In addition to the cell damaging role, recent studies have also shown that ROS participate in cell signaling pathways via reversible oxidation of critical cysteine (Cys) residues of regulatory proteins. The protein arginine methyltransferase (PRMT) family is involved in numerous cell signaling pathways. Our lab has recently discovered that recombinant PRMT1, the major PRMT isoform in humans, is susceptible to oxidation. Oxidized PRMT1 displays much less activity, which can be recovered with the addition of a reductant. This oxidation event involves one or more cysteine residues. We hypothesize that PRMT1 activity could be regulated in vivo depending on the redox state. Therefore, we set out to determine the location(s) of oxidation on PRMT1, the effect on PRMT1 activity and oligomeric state, and the consequences of oxidative stress for in vivo PRMT1 activity and substrate selection.

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