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. 2022 Oct 3;119(41):e2208708119. doi: 10.1073/pnas.2208708119

Fig. 2.

Fig. 2.

phyA2 and phyA3 interacted with and mediated the degradation of LUX1 and LUX2. (A) Yeast two-hybrid assays showing that phyA2 and phyA3 interacted with LUX1, LUX2, E1la, and E1lb. (B) Co-IP assays showing that phyA2 and phyA3 interacted with LUX1 and LUX2 in vivo. (C) Cell-free in vitro degradation system indicating that LUX2-MBP is stabilized in protein extracts from phyA2 phyA3 plants. Anti-actin was used as a sample loading control. Since the other bands were inconsistent when initially added, the bands shown by the red triangles were used to compare strengths. (D) Transient expression in Nicotiana benthamiana leaves demonstrating that phyA2 and phyA3 mediate the degradation of LUX1 and LUX2 in plants. Anti-actin was used as a sample loading control.