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硫酯酶 APT1 是一种双向调节的氧化还原传感器。

The thioesterase APT1 is a bidirectional-adjustment redox sensor.

机构信息

State Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.

Institute for Agricultural Biosciences, Oklahoma State University, Ardmore, OK, 73401, USA.

出版信息

Nat Commun. 2023 May 17;14(1):2807. doi: 10.1038/s41467-023-38464-y.

DOI:10.1038/s41467-023-38464-y
PMID:37198152
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10192129/
Abstract

The adjustment of cellular redox homeostasis is essential in when responding to environmental perturbations, and the mechanism by which cells distinguish between normal and oxidized states through sensors is also important. In this study, we found that acyl-protein thioesterase 1 (APT1) is a redox sensor. Under normal physiological conditions, APT1 exists as a monomer through S-glutathionylation at C20, C22 and C37, which inhibits its enzymatic activity. Under oxidative conditions, APT1 senses the oxidative signal and is tetramerized, which makes it functional. Tetrameric APT1 depalmitoylates S-acetylated NAC (NACsa), and NACsa relocates to the nucleus, increases the cellular glutathione/oxidized glutathione (GSH/GSSG) ratio through the upregulation of glyoxalase I expression, and resists oxidative stress. When oxidative stress is alleviated, APT1 is found in monomeric form. Here, we describe a mechanism through which APT1 mediates a fine-tuned and balanced intracellular redox system in plant defence responses to biotic and abiotic stresses and provide insights into the design of stress-resistant crops.

摘要

细胞氧化还原稳态的调节对于应对环境胁迫至关重要,细胞通过传感器区分正常和氧化状态的机制也很重要。在这项研究中,我们发现酰基蛋白硫酯酶 1 (APT1) 是一种氧化还原传感器。在正常生理条件下,APT1 作为单体存在,通过 C20、C22 和 C37 上的 S-谷胱甘肽化抑制其酶活性。在氧化条件下,APT1 感知氧化信号并四聚化,使其具有功能。四聚体 APT1 去棕榈酰化 S-乙酰化 NAC(NACsa),NACsa 通过上调甘油醛 1 表达转移到细胞核,增加细胞谷胱甘肽/氧化谷胱甘肽(GSH/GSSG)比值,并抵抗氧化应激。当氧化应激减轻时,发现 APT1 呈单体形式。在这里,我们描述了 APT1 在植物生物和非生物胁迫防御反应中调节精细平衡的细胞内氧化还原系统的机制,并为设计抗胁迫作物提供了思路。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/fb6923f8f552/41467_2023_38464_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/d90a0944f380/41467_2023_38464_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/920abadcb8c1/41467_2023_38464_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/05a955e75e95/41467_2023_38464_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/be938e4f5327/41467_2023_38464_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/8e03e3cc7b2a/41467_2023_38464_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/fb6923f8f552/41467_2023_38464_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/d90a0944f380/41467_2023_38464_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/920abadcb8c1/41467_2023_38464_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/05a955e75e95/41467_2023_38464_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/be938e4f5327/41467_2023_38464_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/8e03e3cc7b2a/41467_2023_38464_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/14c1/10192129/fb6923f8f552/41467_2023_38464_Fig6_HTML.jpg

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