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

IF 3.6 Plant signaling & behavior Pub Date : 2025-12-01 Epub Date: 2025-02-26 DOI:10.1080/15592324.2025.2470775
Sidratul Nur Muntaha, Joerg Fettke
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Abstract

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.

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在酵母双杂交筛选中,淀粉 2 和质体磷酸化酶 1 的蛋白质靶向揭示了蛋白质与光合作用蛋白质之间的相互作用。
植物的淀粉代谢涉及一个复杂的相互作用的蛋白质网络,这些蛋白质协同工作以确保淀粉的有效合成和降解。这些相互作用对于调节能量储存和释放之间的平衡,适应植物的发育阶段和环境条件至关重要。已经进行了几项研究来调查淀粉代谢复合物中的蛋白质-蛋白质相互作用(PPIs),但仍不可能揭示这一高度调控过程中的所有PPIs。本研究利用酵母双杂交(Y2H)筛选拟南芥叶片cDNA文库来探索PPIs,重点研究淀粉颗粒起始蛋白protein Targeting to Starch 2 (PTST2, At1g27070)和淀粉和麦芽糊精代谢相关蛋白plastidial phospylase 1 (PHS1, EC 2.4.1.1)。对超过100种正相互作用进行了测序,我们发现叶绿体蛋白可能是PTST2和PHS1的相互作用伙伴。其中发现了光合作用蛋白。这些新的相互作用可能揭示了PTST2和PHS1在淀粉代谢和光合作用之间的新作用。淀粉代谢和其他叶绿体功能之间的动态相互作用突出了淀粉在植物生理和适应的更广泛背景下作为能量储存和调节成分的重要性。
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