Insights into the mechanism of phospholipid hydrolysis by plant non-specific phospholipase C

Ruyi Fan, Fen Zhao, Zhou Gong, Yanke Chen, Bao Yang, Chen Zhou, Jie Zhang, Zhangmeng Du, Xuemin Wang, Ping Yin, Liang Guo () and Zhu Liu ()
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Ruyi Fan: Huazhong Agricultural University
Fen Zhao: Huazhong Agricultural University
Zhou Gong: Chinese Academy of Sciences
Yanke Chen: Chinese Academy of Sciences
Bao Yang: Huazhong Agricultural University
Chen Zhou: Huazhong Agricultural University
Jie Zhang: Huazhong Agricultural University
Zhangmeng Du: Huazhong Agricultural University
Xuemin Wang: University of Missouri
Ping Yin: Huazhong Agricultural University
Liang Guo: Huazhong Agricultural University
Zhu Liu: Huazhong Agricultural University

Nature Communications, 2023, vol. 14, issue 1, 1-11

Abstract: Abstract Non-specific phospholipase C (NPC) hydrolyzes major membrane phospholipids to release diacylglycerol (DAG), a potent lipid-derived messenger regulating cell functions. Despite extensive studies on NPCs reveal their fundamental roles in plant growth and development, the mechanistic understanding of phospholipid-hydrolyzing by NPCs, remains largely unknown. Here we report the crystal structure of Arabidopsis NPC4 at a resolution of 2.1 Å. NPC4 is divided into a phosphoesterase domain (PD) and a C-terminal domain (CTD), and is structurally distinct from other characterized phospholipases. The previously uncharacterized CTD is indispensable for the full activity of NPC4. Mechanistically, CTD contributes NPC4 activity mainly via CTDα1-PD interaction, which ultimately stabilizes the catalytic pocket in PD. Together with a series of structure-guided biochemical studies, our work elucidates the structural basis and provides molecular mechanism of phospholipid hydrolysis by NPC4, and adds new insights into the members of phospholipase family.

Date: 2023
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DOI: 10.1038/s41467-023-35915-4

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