H2 S-介导的经典指蛋白的化 阴阳 1
Madison M Worth1, Logan J Badeau1, Abigail D Reitz1
1Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland 21201, United States.
Biochemistry
|February 6, 2026
概括
硫化 (H2S) 修改了阴阳1 (YY1) 指蛋白,影响了它们的DNA结合. 这种持续硫化破坏了YY1Y1的功能.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 基因规则 基因规则
背景情况:
- 阴阳1 (YY1) 是一种经典的指 (ZF) 蛋白调节基因表达,DNA修复和发育.
- 经典的ZFs通过ββ折叠在Zn (II) 结合上结合DNA.
- 新出现的证据表明,ZF可以被硫化 (H2S) 改变,形成硫化.
研究的目的:
- 为了研究YY1由H2S的持续硫化.
- 为了确定H2S诱导的化对YY1的DNA结合能力的影响.
主要方法:
- 使用NBF-Cl/dimedone标签切换试验检测YY1-ZF2,YY1-ZF3和YY1-ZF2-ZF3结构中的化.
- 采用光异性质来评估DNA结合亲和力.
- 使用循环二元论来分析二次结构变化.
- 使用乙和超氧化物脱酶测量超氧化物生产.
主要成果:
- 证实了YY1结构的H2S持续硫化,需要Zn (II) 和O2,其中超氧化物作为中间体.
- 过硫化取消了YY1-ZF2-ZF3与特定促进子序列的DNA结合.
- 与DNA结合的YY1-ZF2-ZF3对H2S修饰表现出抗性,表明具有保护作用.
- H2S破坏了所有测试的YY1结构的二次结构.
结论:
- H2S持续硫化是一种对YY1.1的新型后翻译修改.
- 过硫化对YY1的DNA结合功能产生负面影响,并改变其结构.
- 这些发现揭示了YY1活动的新调节机制,对基因调节和疾病有影响.
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