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• W4286252630 endingPage "102290" @default.
• W4286252630 startingPage "102290" @default.
• W4286252630 abstract "Protein arginine methylation is involved in many biological processes and can be enhanced in cancer. In mammals, these reactions are catalyzed on multiple substrates by a family of nine protein arginine methyltransferases (PRMTs). However, conditions that may regulate the activity of each enzyme and that may help us understand the physiological role of PRMTs have not been fully established. Previous studies had suggested unexpected effects of temperature and ionic strength on PRMT7 activity. Here we examine in detail the effects of temperature, pH, and ionic strength on recombinant human PRMT1, PRMT5, and PRMT7. We confirmed the unusual temperature dependence of PRMT7, where optimal activity was observed at 15 °C. On the other hand, we found that PRMT1 and PRMT5 are most active near physiological temperatures of 37 °C. However, we showed all three enzymes still have significant activity at 0 °C. Furthermore, we determined that PRMT1 is most active at a pH of about 7.7, while PRMT5 activity is not dependent on pH in the range of 6.5 to 8.5. Significantly, PRMT7 is most active at an alkaline pH of 8.5 but shows little activity at the physiological intracellular pH of about 7.2. We also detected decreased activity at physiological salt conditions for PRMT1, PRMT5, and PRMT7. We demonstrate that the loss of activity is due to the increasing ionic strength. Taken together, these results open the possibility that PRMTs respond in cells undergoing temperature, salt, or pH stress and demonstrate the potential for in vivo regulation of protein arginine methylation." @default.
• W4286252630 created "2022-07-21" @default.
• W4286252630 creator A5025928697 @default.
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• W4286252630 date "2022-09-01" @default.
• W4286252630 modified "2023-10-16" @default.
• W4286252630 title "Human protein arginine methyltransferases (PRMTs) can be optimally active under nonphysiological conditions" @default.
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• W4286252630 doi "https://doi.org/10.1016/j.jbc.2022.102290" @default.
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