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. 2022 Apr 8;13:851531. doi: 10.3389/fpls.2022.851531

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Copyright © 2022 Lu, Li, Peng, Cao, Qu, Sun, Yang, Lu, Zhang, Zheng, Fu and Yu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The dephosphorylation assay in vitro. (A) ZmPP2C26L dephosphorylates ZmMAPK3 and ZmMAPK7. (B) ZmPP2C26S dephosphorylates ZmMAPK3. The phospho-ZmMAPK3/-ZmMAPK7 with HA tag was extracted from maize protoplasts, incubated with His-ZmPP2C26L/His-ZmPP2C26S, separated by 12.5% phos-tag SDS-PAGE gel (top panel) or normal SDS-PAGE gel (middle panel), and detected by using an anti-HA or anti-His antibody. Different amounts of His-ZmPP2C26L/His-ZmPP2C26S were used to dephosphorylate ZmMAPK3 and ZmMAPK7. 1×, 2×, and 4× represent 0.25, 0.5, and 1.0 μg purified His-ZmPP2C26L/-ZmPP2C26S, respectively. + and - denote the presence and absence of the protein in each sample, respectively. The relative intensity of the protein bands was measured using ImageJ, and the lane without His-ZmPP2C26L/His-ZmPP2C26S was set to 1.00.