Key residues for maintaining architecture, assembly of plant hormone SA receptor NPR1
Key residues for maintaining architecture, assembly of plant hormone SA receptor NPR1
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维持植物激素SA受体NPR1结构和组装的关键残基
DOI：
10.1016/j.bbrc.2022.04.119
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发表时间：
2022
影响因子：
3.1
通讯作者：
Hanchi Yan
中科院分区：
文献类型：
--
作者：
Chaoguang Ji;Wenbo Yang;Yongan Wang;Chunlin Su;Xiaorui Li;Peiyuan Liu;Hanchi Yan
水杨酸（SA）是植物对许多病原菌产生抗性所需的关键激素。NPR1（Nonexpressor of patho致病相关基因1）是一种SA受体，在植物的免疫应答中起着关键的调控作用。NPR1的功能依赖于其低聚物到单体的改变。近年来的研究证实，NPRs感知SA并调控下游防御基因的表达，但NPR1寡聚物向单体转化的机制尚不清楚。本文主要研究了NPR1的寡聚化。通过对BTB结构域一些参与蛋白相互作用的残基进行突变实验，我们发现残基His80在NPR1的寡聚化中起关键作用。我们还发现NPR1以接近1:1的比例与锌离子相互作用，与残基His80无关。这些发现有助于我们理解NPR1的构象转换。
Salicylic acid (SA) is a pivotal hormone required for the development of resistance to many pathogens in plants. As an SA receptor, NPR1(Nonexpressor of Pathogenesis-Related Genes 1) plays a key regulatory role in the plant immune response. The function of NPR1 is dependent on the alteration of its oligomer-to-monomer. Research in recent years has proven that NPRs perceive SA and regulate the expression of downstream defense genes, but the mechanism of NPR1 oligomer-to-monomer conversion remains unclear. In this paper, we mainly studied the oligomerization of NPR1. By mutation experiments on some residues in the BTB domain involved in protein interactions, we found that the residue His80 plays a key role in the oligomerization of NPR1. We also found that NPR1, interacting with zinc ions at a ratio close to 1:1, was independent of the residue His80. These findings may help us to understand the conformational conversion of NPR1.