Jurado-Flores Ana, Romero Luis C, Gotor Cecilia
Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, 41092 Sevilla, Spain.
Antioxidants (Basel). 2021 Mar 24;10(4):508. doi: 10.3390/antiox10040508.
Hydrogen sulfide (HS)-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 posttranslational modification of cysteine residues to form a persulfidated thiol motif. We developed a comparative and label-free quantitative proteomic analysis approach for the detection of endogenous persulfidated proteins in N-starved roots by using the tag-switch method. In this work, we identified 5214 unique proteins from root tissue that were persulfidated, 1674 of which were quantitatively analyzed and found to show altered persulfidation levels in vivo under N deprivation. These proteins represented almost 13% of the entire annotated proteome in Arabidopsis. Bioinformatic analysis revealed that persulfidated proteins were involved in a wide range of biological functions, regulating important processes such as primary metabolism, plant responses to stresses, growth and development, RNA translation and protein degradation. Quantitative mass spectrometry analysis allowed us to obtain a comprehensive view of hydrogen sulfide signaling via changes in the persulfidation levels of key protein targets involved in ubiquitin-dependent protein degradation and autophagy, among others.
硫化氢（HS）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，以形成过硫化硫醇基序。我们开发了一种比较性的、无标记的定量蛋白质组学分析方法，通过标签切换法检测缺氮根中内源性过硫化蛋白质。在这项工作中，我们从根组织中鉴定出5214种独特的过硫化蛋白质，其中1674种经过定量分析，发现在缺氮条件下其体内过硫化水平发生了变化。这些蛋白质占拟南芥整个注释蛋白质组的近13%。生物信息学分析表明，过硫化蛋白质参与了广泛的生物学功能，调节着诸如初级代谢、植物对胁迫的反应、生长和发育、RNA翻译以及蛋白质降解等重要过程。定量质谱分析使我们能够通过泛素依赖性蛋白质降解和自噬等过程中关键蛋白质靶点过硫化水平的变化，全面了解硫化氢信号传导。
