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. 2022 Jan 20;9:uhab088. doi: 10.1093/hr/uhab088

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© The Author(s) 2022. Published by Oxford University Press on behalf of Nanjing Agricultural University.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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MRK1 associates with FLS2 and SERK3A/SERK3B in a complex. a Bimolecular fluorescence complementation (BiFC) assays showing MRK1 interaction with FLS2 and SERK3A/SERK3B. MRK1-YFP^N and FLS2-YFP^C or SERK3A/SERK3B-YFP^C were co-transfected into N. benthamiana leaves. The YFP fluorescence was visualized under a confocal microscope at 2 d after transfection. At least two independent experiments were performed with similar results. Bars = 50 μm. b Split-luciferase (LUC) assays showing the interactions of MRK1 with FLS2 and SERK3A/SERK3B. MRK1-nLUC and FLS2-cLUC or SERK3A/SERK3B-cLUC were co-transfected into N. benthamiana leaves. The signal was visualized using a Photek camera. The pseudocolor bar indicates the range of luminescence intensity. These experiments were repeated three times with similar results. c, d Co-immunoprecipitation of MRK1 with FLS2 or SERK3A/SERK3B proteins in N. benthamiana. Proteins were extracted from N. benthamiana leaves expressing MRK1-GFP in combination with FLS2-HA (c) or SERK3A/SERK3B-HA (d) and subjected to immunoprecipitation (IP) with GFP-trap beads followed by immunoblotting with anti-HA antibody. EV-GFP was used as a negative control. These experiments were performed twice with similar results.