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过硫化蛋白质组揭示了硫化氢在拟南芥多种生物过程中对蛋白质功能的调节作用。

Persulfidation proteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes in Arabidopsis.

机构信息

Instituto de Bioquímica Vegetal y Fotosíntesis.

Instituto de Investigaciones Química, Consejo Superior de Investigaciones Científicas y Universidad de Sevilla, Avenida Américo Vespucio, 49, 41092 Sevilla, Spain.

出版信息

J Exp Bot. 2017 Oct 13;68(17):4915-4927. doi: 10.1093/jxb/erx294.

DOI:10.1093/jxb/erx294
PMID:28992305
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5853657/
Abstract

Hydrogen sulfide-mediated signaling pathways regulate many physiological and pathophysiological processes in mammalian and plant systems. The molecular mechanism by which hydrogen sulfide exerts its action involves the post-translational modification of cysteine residues to form a persulfidated thiol motif, a process called protein persulfidation. We have developed a comparative and quantitative proteomic analysis approach for the detection of endogenous persulfidated proteins in wild-type Arabidopsis and L-CYSTEINE DESULFHYDRASE 1 mutant leaves using the tag-switch method. The 2015 identified persulfidated proteins were isolated from plants grown under controlled conditions, and therefore, at least 5% of the entire Arabidopsis proteome may undergo persulfidation under baseline conditions. Bioinformatic analysis revealed that persulfidated cysteines participate in a wide range of biological functions, regulating important processes such as carbon metabolism, plant responses to abiotic and biotic stresses, plant growth and development, and RNA translation. Quantitative analysis in both genetic backgrounds reveals that protein persulfidation is mainly involved in primary metabolic pathways such as the tricarboxylic acid cycle, glycolysis, and the Calvin cycle, suggesting that this protein modification is a new regulatory component in these pathways.

摘要

硫化氢介导的信号通路调节哺乳动物和植物系统中的许多生理和病理生理过程。硫化氢发挥作用的分子机制涉及半胱氨酸残基的翻译后修饰,形成过硫化巯基基序,这一过程称为蛋白质过硫化。我们开发了一种比较和定量蛋白质组学分析方法,用于使用标记转换法检测野生型拟南芥和 L-半胱氨酸脱硫酶 1 突变体叶片中内源性过硫化蛋白。使用从在受控条件下生长的植物中分离的 2015 年鉴定的过硫化蛋白,因此,在基线条件下,至少 5%的整个拟南芥蛋白质组可能经历过硫化。生物信息学分析表明,过硫化半胱氨酸参与广泛的生物学功能,调节重要过程,如碳代谢、植物对非生物和生物胁迫的反应、植物生长和发育以及 RNA 翻译。在两种遗传背景下的定量分析表明,蛋白质过硫化主要涉及三羧酸循环、糖酵解和卡尔文循环等主要代谢途径,表明这种蛋白质修饰是这些途径中的一个新的调节成分。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55f0/5853657/d810c29c25b2/erx29405.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55f0/5853657/0c9527428d2c/erx29401.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55f0/5853657/e5be92dc51c3/erx29402.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55f0/5853657/42f2d6a6280e/erx29403.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55f0/5853657/0334f249c19d/erx29404.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55f0/5853657/d810c29c25b2/erx29405.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55f0/5853657/0c9527428d2c/erx29401.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55f0/5853657/e5be92dc51c3/erx29402.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55f0/5853657/42f2d6a6280e/erx29403.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55f0/5853657/0334f249c19d/erx29404.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55f0/5853657/d810c29c25b2/erx29405.jpg

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