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. 2020 Feb 19;21(4):1419. doi: 10.3390/ijms21041419

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Redox components regulate DCL4 and RTL1 activities. (a) Processing of siRNA precursors by DCL4 requires dsRNA-binding protein (DRB), especially DRB4. GSH and TRXs are able to restore DCL4 activity from the inactive state. Activated DCL4 promotes 21 nt siRNA production. (b) GSSG/GRXs influence RTL1 activity. RTL1 has RNase III domain and dsRNA binding domains (dsRBD), and acts dimers to perform functions. GSSG treatment results in RTL1 glutathionylation at Cys230 position and inhibits its activity. RTL1 activity is restored by glutaredoxin proteins (GRXs). RTL1 negatively regulates siRNA production prior to DCL–mediated cleavage of the siRNA precursors. The dashed line indicates uncharacterized regulation.