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Leaky expression of PRMT1 in Escherichia coli and redox regulation of its histone methyltransferase activity

Kim et al. | Oct 07, 2026

Leaky expression of PRMT1 in <i>Escherichia coli</i> and redox regulation of its histone methyltransferase activity

This study characterizes recombinant human Protein arginine methyltransferase 1 (PRMT1) expressed in Escherichia. coli and reveals that the enzyme exhibits leaky expression even without isopropyl β-D-1-thiogalactopyranoside (IPTG) induction. Through in vitro histone methyltransferase assays, we demonstrate that PRMT1 activity toward histone H4R3 is enhanced by dithiothreitol (DTT) in a dose-dependent manner but remains unresponsive to β-mercaptoethanol. These findings highlight the critical role of redox conditions in regulating PRMT1 catalytic function and provide a practical framework for future biochemical and kinetic studies.

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Quantifying natural recovery of dopamine deficits induced by chronic stress

Josyula et al. | Oct 27, 2025

Quantifying natural recovery of dopamine deficits induced by chronic stress
Image credit: Shawn Day

Here the authors investigated the natural recovery of stress-induced dopamine-related gene deficits in C. elegans by measuring the expression of cat-2 (dopamine biosynthesis) and sod-2 (oxidative stress) following exposure to starvation or hydrocortisone. They found that the reversibility of sod-2 and the expression of cat-2 were highly dependent on the type and severity of the stressor, suggesting that the body's natural ability to recover from dopamine dysfunction has biological limitations.

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