Nt-acetylation-independent turnover of SQUALENE EPOXIDASE 1 by Arabidopsis DOA10-like E3 ligases.
Nt-acetylation-independent turnover of SQUALENE EPOXIDASE 1 by Arabidopsis DOA10-like E3 ligases.
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拟南芥doa10样E3连接酶对小乙烯环氧酶1的NT-乙酰化非依赖性周转。
DOI：
10.1093/plphys/kiad406
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发表时间：
2023-10-26
期刊：
影响因子：
7.4
通讯作者：
Gibbs, Daniel J.
中科院分区：
文献类型：
--
作者：
Etherington, Ross D.;Bailey, Mark;Boyer, Jean-Baptiste;Armbruster, Laura;Cao, Xulyu;Coates, Juliet C.;Meinnel, Thierry;Wirtz, Markus;Giglione, Carmela;Gibbs, Daniel J.
乙酰化依赖性（Ac/）N-降解决定子途径通过被称为Ac/N-识别蛋白的E3连接酶识别其乙酰化N-末端（Nt）来降解蛋白质。迄今为止，在植物中尚未定义特定的Ac/N-识别。在这里，我们使用分子，遗传学和多组学方法来表征拟南芥（拟南芥）的潜在作用，降解的ALPHA 2 10（DOA 10）样E3连接酶在NT-乙酰化-（NTA）-依赖性营业额的蛋白质在全球和蛋白质特异性尺度。拟南芥有两个内质网（ER）定位的DOA 10样蛋白。AtDOA 10A，而不是酿酒酵母科特异性AtDOA 10 B，可以补偿酵母（酿酒酵母）ScDOA 10功能的丧失。Atdoa 10 a/B RNAi突变体的转录组和Nt-乙酰组分析显示，与野生型相比，整体NTA谱没有明显差异，表明AtDOA 10 s不调节NTA底物的批量周转。使用蛋白质稳态和环己酰亚胺追逐降解试验在酵母和拟南芥中，我们表明，营业额的ER定位角鲨烯表氧化酶1（AtSQE 1），一个关键的甾醇生物合成酶，介导的AtDOA 10。AtSQE 1在植物中的降解不依赖于NTA，但NT-乙酰基转移酶间接影响其在酵母中的周转，表明NTA和细胞蛋白质稳态的王国特异性差异。我们的工作表明，与酵母和哺乳动物相比，靶向NT-乙酰化蛋白不是拟南芥中DOA 10样E3连接酶的主要功能，并为植物ERAD和真核生物中控制甾醇生物合成的调控机制的保护提供了进一步的见解。全局和蛋白质特异性分析表明，拟南芥DOA 10A样E3连接酶调节角鲨烯表氧化酶1的营业额独立的Ac/N-降解决定子途径。
The acetylation-dependent (Ac/)N-degron pathway degrades proteins through recognition of their acetylated N-termini (Nt) by E3 ligases called Ac/N-recognins. To date, specific Ac/N-recognins have not been defined in plants. Here we used molecular, genetic, and multiomics approaches to characterize potential roles for Arabidopsis (Arabidopsis thaliana) DEGRADATION OF ALPHA2 10 (DOA10)-like E3 ligases in the Nt-acetylation-(NTA)-dependent turnover of proteins at global- and protein-specific scales. Arabidopsis has two endoplasmic reticulum (ER)-localized DOA10-like proteins. AtDOA10A, but not the Brassicaceae-specific AtDOA10B, can compensate for loss of yeast (Saccharomyces cerevisiae) ScDOA10 function. Transcriptome and Nt-acetylome profiling of an Atdoa10a/b RNAi mutant revealed no obvious differences in the global NTA profile compared to wild type, suggesting that AtDOA10s do not regulate the bulk turnover of NTA substrates. Using protein steady-state and cycloheximide-chase degradation assays in yeast and Arabidopsis, we showed that turnover of ER-localized SQUALENE EPOXIDASE 1 (AtSQE1), a critical sterol biosynthesis enzyme, is mediated by AtDOA10s. Degradation of AtSQE1 in planta did not depend on NTA, but Nt-acetyltransferases indirectly impacted its turnover in yeast, indicating kingdom-specific differences in NTA and cellular proteostasis. Our work suggests that, in contrast to yeast and mammals, targeting of Nt-acetylated proteins is not a major function of DOA10-like E3 ligases in Arabidopsis and provides further insight into plant ERAD and the conservation of regulatory mechanisms controlling sterol biosynthesis in eukaryotes. Global- and protein-specific analyses reveal that Arabidopsis DOA10A-like E3 ligases regulate the turnover of SQUALENE EPOXIDASE 1 independently of the Ac/N-degron pathway.
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DOI：
10.1073/pnas.1718336115
发表时间：
2018-04-24
影响因子：
11.1
作者：
Drazic A;Aksnes H;Marie M;Boczkowska M;Varland S;Timmerman E;Foyn H;Glomnes N;Rebowski G;Impens F;Gevaert K;Dominguez R;Arnesen T
通讯作者：
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影响因子：
2.9
作者：
Abas L;Luschnig C
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影响因子：
27.5
作者：
Gong, Xiaodi;Huang, Yaqian;Wang, Yonghong
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Wang, Yonghong
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影响因子：
11.6
作者：
Cui, Feng;Liu, Lijing;Xie, Qi
通讯作者：
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影响因子：
7
作者：
Bienvenut, Willy V.;Sumpton, David;Giglione, Carmela
通讯作者：
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