Skip to main content
. 2019 Feb 19;93(5):e01635-18. doi: 10.1128/JVI.01635-18

FIG 5.

FIG 5

TGBp2 interacts with PVX RdRp. (A) Schematic representations of the PVX RdRp domains. MET, methyltransferase domain; UNL, unstructured loop domain; HEL, helicase domain; REP, replicase domain; RepN, N terminus of the REP domain; RepC, C terminus of the REP domain. The numbers represent the amino acid positions of the domain boundaries. (B) Subcellular localization of MET-YFP, UNL-YFP, HEL-YFP, and REP-YFP in N. benthamiana epidermal cells at 48 hpi. The insets show the typical cytoplasmic granules of MET-YFP and HEL-YFP, as well as the nuclear signal of UNL-YFP and REP-YFP. (C) BiFC for protein-protein interactions between TGBp2 and RdRp domains in N. benthamiana epidermal cells at 48 hpi. Micrographs were obtained using the same settings. Scale bars = 50 μm. (D) Subcellular localization of RepN-YFP and RepC-YFP in N. benthamiana epidermal cells at 48 hpi. The insets show the typical nuclear signal of RepN-YFP and cytoplasmic vesicles of RepC-YFP. The nuclei are indicated by white asterisks, and the typical vesicle-like structures are indicated by white arrowheads. Scale bars = 50 μm. (E) BiFC for protein-protein interactions between TGBp2 and RepN or RepC. Micrographs were obtained using the same parameters. Scale bars = 50 μm. (F) MYTH for protein-protein interaction between TGBp2 and RdRp domains. (G) Influence of TGBp2 on the subcellular localization of RdRp and REP domain in N. benthamiana epidermal cells at 48 dpi. RdRp-YFP and REP-YFP are shown in green, and mRFP-TGBp2 is shown in red. Scale bars = 50 μm.