In Arabidopsis, a family of six arogenate dehydratases (ADTs) has been identified which catalyze the terminal step of phenylalanine biosynthesis. ADTs share considerable sequence similarity to bacterial prephenate dehydratases, which form homodimers. The protein-protein interaction profiles of Arabidopsis ADTs were characterized using Yeast-2-Hybrid and Bi-molecular Fluorescence Complementation approaches. Results show that ADT1, but not ADT2, is able to form homo- and heterodimers with all other ADTs in yeast. In contrast, all six ADTs form all possible homo- and heterodimer combinations in ptanta, where they display two different subcellular localization patterns. Most ADT dimers localize to the chloroplast in a stromule-like pattern, but ADT5 dimers also localize in a nuclear-like pattern. Large scale cDNA library screens also identified a number of other putative interactors, suggesting that ADTs may be part of a larger protein complex. This study is the first to characterize the protein-protein interaction profiles of plant ADTs
