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. 2021 Sep 23;12:5614. doi: 10.1038/s41467-021-25909-5

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — GST pulldown results showing that PIF3mAD, like PIF3, interacts preferentially with active PHYA and PHYB. GST pulldown assays were performed using recombinant GST-PIF3, GST-PIF3mAD, or GST to pull down in vitro translated HA-tagged PHYA (PHYA-HA) or PHYB (PHYB-HA) conjugated with a phycocyanobilin chromophore. The pulldown assays were performed in either R or FR light to maintain PHYA-HA and PHYB-HA in the Pfr or Pr conformer, respectively. Input and bound PHYA-HA and PHYB-HA fractions were detected via immunoblots (upper panels) using anti-HA antibodies. Immobilized GST, GST-PIF3, and GST-PIF3mAD are shown in the Coomassie Brilliant Blue-stained SDS-PAGE gels (lower panels). The source data underlying the immunoblots and Coomassie Brilliant Blue-stained SDS-PAGE gels are provided in the Source data file.