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Article Addendum

Conserved function of mediator in regulating nuclear hormone receptor activation between plants and animals

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Article: e1403709 | Received 25 Oct 2017, Accepted 31 Oct 2017, Published online: 22 Jun 2018

Figures & data

Figure 1. MED25 interacts with a subset of JAZ proteins. (A) Y2H assays show the interaction of MED25 with JAZ proteins. Transformed yeast strains were plated on SD medium lacking His, Ade, Leu, and Trp (SD/−4). (B) MED25 interacts with JAZ1 in LCI assays. (Top) LUC images of N. benthamiana leaves coinfiltrated with the different construct combinations are shown in the lower quadrant of the circle. (C) and (D) Mapping of the protein domains involved in MED25-JAZ1 interaction using LCI assays. (C) Based on the schematic protein structure of MED25, full-length MED25 or its derivatives (MED25-nLUC or MED25-nLUC derivatives) were tested for interactions with JAZ1 (cLUC-JAZ1). N. benthamiana leaves co-transformed with MED25-nLUC or MED25-nLUC derivatives and cLUC-JAZ1 were imaged 72 h after Agrobacterium infiltration. (D) Based on the schematic protein structure of JAZ1, full-length JAZ1 or its derivatives (cLUC-JAZ1 or cLUC-JAZ1 derivatives) were tested for interaction with MED25 (MED25-nLUC). N. benthamiana leaves co-transformed with cLUC-JAZ1 or cLUC-JAZ1 derivatives and MED25-nLUC were imaged 72 h after Agrobacterium infiltration.

Figure 1. MED25 interacts with a subset of JAZ proteins. (A) Y2H assays show the interaction of MED25 with JAZ proteins. Transformed yeast strains were plated on SD medium lacking His, Ade, Leu, and Trp (SD/−4). (B) MED25 interacts with JAZ1 in LCI assays. (Top) LUC images of N. benthamiana leaves coinfiltrated with the different construct combinations are shown in the lower quadrant of the circle. (C) and (D) Mapping of the protein domains involved in MED25-JAZ1 interaction using LCI assays. (C) Based on the schematic protein structure of MED25, full-length MED25 or its derivatives (MED25-nLUC or MED25-nLUC derivatives) were tested for interactions with JAZ1 (cLUC-JAZ1). N. benthamiana leaves co-transformed with MED25-nLUC or MED25-nLUC derivatives and cLUC-JAZ1 were imaged 72 h after Agrobacterium infiltration. (D) Based on the schematic protein structure of JAZ1, full-length JAZ1 or its derivatives (cLUC-JAZ1 or cLUC-JAZ1 derivatives) were tested for interaction with MED25 (MED25-nLUC). N. benthamiana leaves co-transformed with cLUC-JAZ1 or cLUC-JAZ1 derivatives and MED25-nLUC were imaged 72 h after Agrobacterium infiltration.

Figure 2. Analogy of nuclear hormone receptor activation system between plants and mammals. The “COI1-JAZ-MYC2” module of JA signaling in plants resembles the nuclear hormone receptor RAR in mammals. In plants, MED25 interacts with COI1 and JAZ proteins and facilitates JA-Ile-triggered degradation of JAZ proteins, which in turn enhances the MED25-MYC2 interaction. MED25 functions in chromatin modification and preinitiation complex assembly by recruiting HAC1 and the Mediator complex, respectively, to MYC2-targeted promoters. In mammals, MED25 interacts with RAR in the presence of RA and functions in chromatin modification and preinitiation complex by recruiting CBP1 and the Mediator complex, respectively, to RAR-responsive promoters.

Figure 2. Analogy of nuclear hormone receptor activation system between plants and mammals. The “COI1-JAZ-MYC2” module of JA signaling in plants resembles the nuclear hormone receptor RAR in mammals. In plants, MED25 interacts with COI1 and JAZ proteins and facilitates JA-Ile-triggered degradation of JAZ proteins, which in turn enhances the MED25-MYC2 interaction. MED25 functions in chromatin modification and preinitiation complex assembly by recruiting HAC1 and the Mediator complex, respectively, to MYC2-targeted promoters. In mammals, MED25 interacts with RAR in the presence of RA and functions in chromatin modification and preinitiation complex by recruiting CBP1 and the Mediator complex, respectively, to RAR-responsive promoters.