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. 2022 Nov 30;13:1065253. doi: 10.3389/fpls.2022.1065253

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Copyright © 2022 Li, Liu, Mei, Jiang, Lv, Zhai and Li

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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OCP physically interacts with OsRACK1A or OsSNAP32. (A) OCP and its truncations interact with OsRACK1A or OsSNAP32 in Y2H. AD, pGADT7; BD, pGBKT7; BD-OCP, full length of OCP; BD-OCP-1, 1–110 amino acid (aa) of OCP; BD-OCP-2, 111–348 aa; BD-OCP-3, 349–458 aa; BD-OCP-4, 1–348 aa; BD-OCP-5, 111–458 aa. 20 mM 3-amino-1,2,4-triazole (3-AT) was added to BD-OCP-3 and BD-OCP-5. (B) BiFC assay showing the interaction of OCP with OsRACK1A or OsSNAP32 in tobacco leaf epidermal cells. nYFP+cYFP-OCP was the negative control. Bar = 20 μm. (C) Co-immunoprecipitation assays to verify the interaction of OCP with OsRACK1A or OsSNAP32 in rice protoplasts. OCP-Myc+mCherry was the negative control. OsRACK1A-mCherry and OsSNAP32-mCherry were detected with Anti-mCherry.