Fig. 2: The protein–protein interaction among the phosphoglycerate mutase 1–enolase–PK4 complex and VDAC. | Nature Communications

Fig. 2: The protein–protein interaction among the phosphoglycerate mutase 1–enolase–PK4 complex and VDAC.

From: A moonlighting role for enzymes of glycolysis in the co-localization of mitochondria and chloroplasts

Fig. 2

a mCitrine-TPT/PGAM1-mcherry. b Enolase-mCitrine/PGAM1-mcherry. c Enolase-mCitrine/PGAM2-mcherry. d Enolase-mCitrine/PYK4-mcherry. e VDAC1-mCitrine/PYK4-mcherry. f VDAC3-mCitrine/PYK4-mcherry. Co-sublocalization of phosphoglycerate mutase 1–enolase–PYK4 complex with organelles’ membrane protein was further tested by confocal with transient expression of tagged proteins in Arabidopsis leaves. The panels from the left side show the mCitrine fluorescence, mCherry fluorescence autofluorescence, blank, and the merged image of all of those, respectively. g Confirmation of protein–protein interaction by FLIM-FRET assays. All the vectors of the co-sublocalization were transformed into plant cell culture for the FLIM-FRET analysis. The Los2-mcitrine/mCherry was used as negative control (*P < 0.05, error bar is SEM with more than 10 replicates).

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