Bimolecular Fluorescence Complementation Assay Showing That BAM1 and LSF1 Interact in the Chloroplast. Bimolecular Fluorescence Complementation Assay Showing.

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Bimolecular Fluorescence Complementation Assay Showing That BAM1 and LSF1 Interact in the Chloroplast. Bimolecular Fluorescence Complementation Assay Showing That BAM1 and LSF1 Interact in the Chloroplast. C-terminal fusion constructs of BAM1 and LSF1 with N-terminal (YN) and C-terminal (YC) parts of YFP were cotransformed into N. benthamiana leaf cells using A. tumefaciens. Fusion constructs of the RbcS transit peptide (AtS1b) were used as negative controls for YFP self-assembly. YFP and chlorophyll fluorescence were assayed 72 h after infiltration using a confocal microscope. Fluorescence signals were overlaid onto a bright field image (YFP and Chlorophyll) and an image merging both YFP and chlorophyll fluorescence (Merge) was obtained using the Leica Application Suite software. Tina B. Schreier et al. Plant Cell 2019;31:2169-2186 ©2019 by American Society of Plant Biologists