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Fig. 2. The formation of the Arabidopsis Min complex. (A) Yeast two-hybrid analysis of AtMinE1 and AtMinD1 interactions. Domains are represented as follows: TP, transit peptide; AMD, anti-MinCD domain; hatched box, AtMinD1-interacting domain; TSD, topological specificity domain; red arrow, -sheet; red cylinder, -helix; CTE, C-terminal extension. Full-length AtMinE1 or AtMinD1 fused to the GAL4 DNA-binding domain (BD) and truncations of AtMinE1 fused to the GAL4 activation domain (AD) were expressed in HF7c yeast cells and monitored for growth on synthetic drop-out media lacking tryptophan and leucine (–TL) and synthetic drop-out media lacking tryptophan, leucine and histidine (–HTL). Relative interaction strengths are represented as three classes based on the ratio of growth on –TL to –HTL: ++, ratio of 0.6-1.0; +, ratio of 0.3-0.6; –, ratio equal to the relevant control (<0.3 in all cases). (B) BiFC assays. AtMinE1 and AtMinD1 were fused to the non-fluorescent YFP_155-238 (CY) and were coexpressed in tobacco chloroplasts with truncations of AtMinE1 fused to YFP_1-154 (NY). Interactions of the full-length AtMinE1 and AtMinD1 fusions were used as positive controls. Extended-focus images of reconstituted YFP fluorophore (YFP) and chlorophyll autofluorescence (chlorophyll) were captured by epifluorescence microscopy using Volocity II software. Bar, 5 µm; +, positive reconstitution of YFP; –, no reconstitution of YFP.

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