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Residues Clustered in the Light-Sensing Knot of Phytochrome B are Necessary for Conformer-Specific Binding to Signaling Partner PIF3

Figure 8

The Two Class II phyB Missense Mutations Tested Abolish Binding to Multiple bHLH PIFs.

A) Co-immunoprecipition assays of the full-length phyB G111D mutant compared to wild type phyB for interaction with PIF1, PIF3, PIF4, PIF5, and PIF7. B) Quantification of the interaction of the phyB G111D mutant with the bHLHs shown in panel A. Green bars represent binding of the wild-type phyB and blue bars represent binding of the mutant. Interaction of the wild-type phyB Pr with GAD-PIF3 is set equal to one. C) Co-immunoprecipitation assays of the full-length phyB R352K mutant compared to wild-type phyB for interaction with PIF1, PIF3, PIF4, PIF5, and PIF7. D) Quantification of the interaction of the phyB R352K mutant with the bHLHs shown in panel C. Green bars represent binding of the wild-type phyB and blue bars represent binding of the mutant. Interaction of the wild-type phyB Pr with GAD-PIF3 is set equal to one.

Figure 8

doi: https://doi.org/10.1371/journal.pgen.1000352.g008