DJ-1 is a highly conserved soluble protein that is associated to several cellular pathways. In humans, DJ-1 has been implicated in several pathologies such as cancer, Parkinson’s disease and amyotrophic lateral sclerosis. Several roles have been attributed to DJ-1, including defense against oxidative stress, chaperone activity and proteasome regulation. The recent finding that DJ-1 acts as a protein and DNA deglycase further confirms the protective function of DJ-1 and suggests a common mechanism of action in the various pathways in which DJ-1 is involved. Cysteine 106, located in the putative active site of DJ-1, is critical for the biological activity of DJ-1 and is easily oxidized to cysteine-sulfinate. While such oxidation modulates DJ-1 activity, the underlying molecular mechanism has not yet been elucidated. Cysteine oxidation does not perturb the protein structure, therefore changes in protein dynamics in solution could modulate its function. Here, we report a revised and completed (98%) backbone assignment of reduced DJ-1, together with the backbone assignment of oxidized DJ-1. Chemical shift perturbation is observed in several regions across the sequence, while no changes in secondary structure are observed. These data will provide the starting point for further characterization of the changes in the backbone dynamics of DJ-1 upon oxidation in solution at physiological temperature.

中文翻译：

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人DJ-1处于还原状态和半胱氨酸亚磺酸状态的骨干共振分配。

DJ-1是一种高度保守的可溶性蛋白，与几种细胞途径相关。在人类中，DJ-1与多种疾病有关，例如癌症，帕金森氏病和肌萎缩性侧索硬化症。DJ-1具有多种作用，包括防御氧化应激，伴侣活性和蛋白酶体调控。DJ-1充当蛋白质和DNA脱糖酶的最新发现进一步证实了DJ-1的保护功能，并暗示了DJ-1参与的各种途径的共同作用机制。位于DJ-1假定的活性位点的半胱氨酸106对DJ-1的生物学活性至关重要，并且容易被氧化为半胱氨酸亚磺酸盐。虽然这种氧化调节DJ-1活性，但尚未阐明潜在的分子机制。半胱氨酸氧化不会干扰蛋白质结构，因此溶液中蛋白质动力学的变化可能会调节其功能。在这里，我们报告还原DJ-1的修订和完成（98％）的主干分配，以及氧化DJ-1的主干分配。在整个序列的多个区域中观察到化学位移扰动，而未观察到二级结构的变化。这些数据将为进一步表征生理温度下溶液中氧化后DJ-1的主链动力学变化提供起点。在整个序列的多个区域中观察到化学位移扰动，而未观察到二级结构的变化。这些数据将为进一步表征生理温度下溶液中氧化后DJ-1的主链动力学变化提供起点。在整个序列的多个区域中观察到化学位移扰动，而未观察到二级结构的变化。这些数据将为进一步表征生理温度下在溶液中氧化后DJ-1的主链动力学变化提供起点。