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鸭茅热休克蛋白 90 激活因子具有自主伴侣蛋白特性,并能激活热休克蛋白 90 转录以增强其耐热性。

Orchardgrass ACTIVATOR OF HSP90 ATPASE possesses autonomous chaperone properties and activates Hsp90 transcription to enhance thermotolerance.

机构信息

Department of Plant Medicine, Institute of Agriculture and Life Science, Gyeongsang National University, Jinju, 52828, Republic of Korea.

Grassland & Forages Division, National Institute of Animal Science, Rural Development Administration, Cheonan, 31000, Republic of Korea.

出版信息

Biochem Biophys Res Commun. 2022 Jan 1;586:171-176. doi: 10.1016/j.bbrc.2021.11.080. Epub 2021 Nov 24.

DOI:10.1016/j.bbrc.2021.11.080
PMID:34856417
Abstract

High temperature stress is an environmental factor that negatively affects the growth and development of crops. Hsp90 (90 kDa heat shock protein) is a major molecular chaperone in eukaryotic cells, contributing to the maintenance of cell homeostasis through interaction with co-chaperones. Aha1 (activator of Hsp90 ATPase) is well known as a co-chaperone that activates ATPase activity of Hsp90 in mammals. However, biochemical and physiological evidence relating to Aha has not yet been identified in plants. In this study, we investigated the heat-tolerance function of orchardgrass (Dactylis glomerata L.) Aha (DgAha). Recombinant DgAha interacted with cytosolic DgHsp90s and efficiently protected substrates from thermal denaturation. Furthermore, heterologous expression of DgAha in yeast (Saccharomyces cerevisiae) cells and Arabidopsis (Arabidopsis thaliana) plants conferred thermotolerance in vivo. Enhanced expression of DgAha in Arabidopsis stimulates the transcription of Hsp90 under heat stress. Our data demonstrate that plant Aha plays a positive role in heat stress tolerance via chaperone properties and/or activation of Hsp90 to protect substrate proteins in plants from thermal injury.

摘要

高温胁迫是一种影响作物生长和发育的环境因素。Hsp90(90 kDa 热休克蛋白)是真核细胞中的主要分子伴侣,通过与共伴侣相互作用有助于维持细胞内稳态。Aha1(Hsp90 ATP 酶激活因子)是一种众所周知的共伴侣,在哺乳动物中激活 Hsp90 的 ATP 酶活性。然而,与植物中的 Aha 相关的生化和生理证据尚未被确定。在这项研究中,我们研究了果园草(Dactylis glomerata L.)Aha(DgAha)的耐热功能。重组 DgAha 与细胞质 DgHsp90s 相互作用,并有效地防止底物受热变性。此外,DgAha 在酵母(Saccharomyces cerevisiae)细胞和拟南芥(Arabidopsis thaliana)植物中的异源表达赋予了体内的耐热性。在拟南芥中增强 DgAha 的表达可刺激 Hsp90 在热应激下的转录。我们的数据表明,植物 Aha 通过伴侣特性和/或激活 Hsp90 发挥积极作用,以保护植物中的底物蛋白免受热损伤,从而提高植物对热应激的耐受性。

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Orchardgrass ACTIVATOR OF HSP90 ATPASE possesses autonomous chaperone properties and activates Hsp90 transcription to enhance thermotolerance.鸭茅热休克蛋白 90 激活因子具有自主伴侣蛋白特性,并能激活热休克蛋白 90 转录以增强其耐热性。
Biochem Biophys Res Commun. 2022 Jan 1;586:171-176. doi: 10.1016/j.bbrc.2021.11.080. Epub 2021 Nov 24.
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[Changes in heat shock protein synthesis and thermotolerance of Arabidopsis thaliana seedlings as a result of inhibition of Hsp90 by geldanamycin].[格尔德霉素抑制热休克蛋白90导致拟南芥幼苗热休克蛋白合成及耐热性的变化]
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Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.热休克蛋白 90 伴侣蛋白 Aha1 是酿酒酵母 MAL 激活因子的负调控因子,在伴侣蛋白激活途径中发挥早期作用。
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A highly charged region in the middle domain of plant endoplasmic reticulum (ER)-localized heat-shock protein 90 is required for resistance to tunicamycin or high calcium-induced ER stresses.植物内质网(ER)定位的热休克蛋白90中间结构域中的一个高电荷区域是抵抗衣霉素或高钙诱导的内质网应激所必需的。
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N-terminal arm of orchardgrass Hsp17.2 (DgHsp17.2) is essential for both in vitro chaperone activity and in vivo thermotolerance in yeast.果园草Hsp17.2(DgHsp17.2)的N端臂对于酵母中的体外伴侣活性和体内耐热性均至关重要。
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The cytosolic/nuclear HSC70 and HSP90 molecular chaperones are important for stomatal closure and modulate abscisic acid-dependent physiological responses in Arabidopsis.细胞质/核 HSC70 和 HSP90 分子伴侣对于气孔关闭很重要,并调节拟南芥中依赖脱落酸的生理反应。
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Arabidopsis ROF1 (FKBP62) modulates thermotolerance by interacting with HSP90.1 and affecting the accumulation of HsfA2-regulated sHSPs.拟南芥ROF1(FKBP62)通过与HSP90.1相互作用并影响HsfA2调控的小分子热激蛋白(sHSPs)的积累来调节耐热性。
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