Oxidative post-translational modifications of protein thiols are well recognized as a readily occurring alteration of proteins, which can modify their function and thus control cellular processes. The development of techniques enabling the site-specific assessment of protein thiol oxidation on a proteome-wide scale significantly expanded the number of known oxidation-sensitive protein thiols. However, lacking behind are large-scale data on the redox state of proteins during ageing, a physiological process accompanied by increased levels of endogenous oxidants. Here, we present the landscape of protein thiol oxidation in chronologically aged wild-type Saccharomyces cerevisiae in a time-dependent manner. Our data determine early-oxidation targets in key biological processes governing the de novo production of proteins, protein folding, and degradation, and indicate a hierarchy of cellular responses affected by a reversible redox modification. Comparison with existing datasets in yeast, nematode, fruit fly, and mouse reveals the evolutionary conservation of these oxidation targets. To facilitate accessibility, we integrated the cross-species comparison into the newly developed OxiAge Database.

中文翻译：

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衰老依赖性硫醇氧化揭示了具有核心蛋白质稳态功能的蛋白质的早期氧化。

蛋白质硫醇的氧化翻译后修饰被认为是一种容易发生的蛋白质改变，可以改变其功能，从而控制细胞过程。能够在蛋白质组范围内对蛋白质硫醇氧化进行位点特异性评估的技术的发展显着扩大了已知的氧化敏感蛋白质硫醇的数量。然而，缺乏关于衰老过程中蛋白质氧化还原状态的大规模数据，衰老过程是一个伴随着内源性氧化剂水平增加的生理过程。在这里，我们以时间依赖性方式展示了按时间顺序老化的野生型酿酒酵母中蛋白质硫醇氧化的情况。我们的数据确定了控制蛋白质从头产生、蛋白质折叠和降解的关键生物过程中的早期氧化目标，并表明受可逆氧化还原修饰影响的细胞反应的层次结构。与酵母、线虫、果蝇和小鼠的现有数据集的比较揭示了这些氧化目标的进化保守性。为了方便访问，我们将跨物种比较集成到新开发的 OxiAge 数据库中。