Supporting data for "EXPLORATION OF 3-NITROTYROSINE AND 3-AMINOTYROSINE-CONTAINING PROTEINS WITH A SYNTHETIC PROBE"

In our study, we focus on developing a new method to identify some proteins with tyrosine modifications using synthetic probes. Tyrosine, a vital amino acid that comprises approximately 3.2% of protein composition, is subject to a range of post-translational modifications (PTMs), including nitration, phosphorylation, hydroxylation, halogenation, and sulfation. These PTMs play crucial roles in regulating protein functions, cellular signalling, homeostasis, and a host of biological processes. A well-studied PTM, protein tyrosine nitration (PTN), arises from oxidative and nitrative stress. Therefore, we developed a selective detection method using a synthetic probe to identify proteins with tyrosine modification. Utilizing the probe, we successfully labelled and enriched numerous proteins with tyrosine modifications in RAW264.7 cells. Afterwards, we selected two targets for further investigation into the effects of tyrosine modifications on their functions. By using the purifying site-specific modified proteins, it revealed that tyrosine modification indeed affected protein function at different sites.

本研究致力于开发一种新型方法，以合成探针识别具有酪氨酸修饰的蛋白质。酪氨酸，一种构成蛋白质约3.2%的至关重要的氨基酸，易受多种翻译后修饰（PTMs）的影响，包括硝化、磷酸化、羟基化、卤素化和硫酸化。这些PTMs在调控蛋白质功能、细胞信号传导、稳态平衡以及众多生物学过程中扮演着关键角色。蛋白质酪氨酸硝化（PTN）作为一种研究广泛的PTM，源于氧化和硝化应激。因此，本研究开发了一种选择性检测方法，利用合成探针识别具有酪氨酸修饰的蛋白质。通过使用该探针，我们成功地在RAW264.7细胞中标记并富集了多种具有酪氨酸修饰的蛋白质。随后，我们选取了两个目标进行进一步研究，以探究酪氨酸修饰对其功能的影响。通过使用特定位点修饰的纯化蛋白质，研究揭示了酪氨酸修饰确实在不同位点影响了蛋白质功能。