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. 2019 Jul 10;18(2):337–353. doi: 10.1111/pbi.13201

Figure 7.

Figure 7

MdMYB308L interacts with MdMIEL1. (a) Yeast two‐hybrid assays. The open reading frames of MdMYB308L and MdMIEL1 were fused with pGBD and pGAD vectors, respectively. Transformed yeast cells were grown on SD‐Trp/‐Leu (‐T/‐L), SD‐Trp/‐Leu/‐His/‐Ade (‐T/‐L/‐H/‐A) or SD‐Trp/‐Leu/‐His/‐Ade supplementing X‐gal (‐T/‐L/‐H/‐A+X‐gal) media. (b) Pull‐down assays. E. coli‐expressed HIS or MdMIEL1‐HIS proteins were incubated with a cobalt chelate affinity resin containing the immobilized glutathione‐tagged MdMYB308L protein. The protein mixtures were purified using a glutathione purification kit. (c) Bimolecular fluorescence complementation assays. The open reading frames of MdMIEL1 and MdMYB308L were fused to the N‐terminal part of YFP and the C‐terminal part of YFP, respectively. Bars = 10 μm.