Protein targeting to Starch 2 and the plastidial phosphorylase 1 revealed protein-protein interactions with photosynthesis proteins in yeast two-hybrid screenings.

Starch metabolism in plants involves a complex network of interacting proteins that work together to ensure the efficient synthesis and degradation of starch. These interactions are crucial for regulating the balance between energy storage and release, adapting to the plant's developmental stage and environmental conditions. Several studies have been performed to investigate protein-protein interactions (PPIs) in starch metabolism complexes, yet it remains impossible to unveil all of the PPIs in this highly regulated process. This study uses yeast-two-hybrid (Y2H) screening against the Arabidopsis leaf cDNA library to explore PPIs, focusing on the starch-granule-initiating protein named Protein Targeting to Starch 2 (PTST2, At1g27070) and the protein involved in starch and maltodextrin metabolism, namely, plastidial phosphorylase 1 (PHS1, EC 2.4.1.1). More than 100 positive interactions were sequenced, and we found chloroplastidial proteins to be putative interacting partners of PTST2 and PHS1. Among them, photosynthetic proteins were discovered. These novel interactions could reveal new roles of PTST2 and PHS1 in the connection between starch metabolism and photosynthesis. This dynamic interplay between starch metabolism and other chloroplast functions highlights the importance of starch as both an energy reservoir and a regulatory component in the broader context of plant physiology and adaptation.