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通过序列动机识别的目标选择性蛋白质S-化
Jie Jia1, Abul Arif1, Fulvia Terenzi1
1Department of Cellular and Molecular Medicine, The Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.
Cell
|November 24, 2014
概括
研究人员发现了一种新的蛋白质复合物,该复合物使用氧化 (NO) 来修改蛋白质. 这种复杂的,涉及诱导性氧化合成酶 (iNOS),S100A8和S100A9,精确地准特定的蛋白质位点,类似于酸化.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 细胞信号传递 细胞信号传递
背景情况:
- S-化是一种关键的氧化 (NO) 介导的转化后修饰,调节细胞功能.
- 虽然已知许多S-化蛋白质,但酶 (S-化酶) 和对位点选择性修饰的机制在很大程度上仍未表征.
研究的目的:
- 为了识别和表征新的S-化酶复合体.
- 阐明选择性S-nitrosylation的背后机制.
- 为了识别由S-酸酶识别的序列动图.
主要方法:
- 蛋白质组分析以识别S-化蛋白质.
- 生物化学测试以表征酶活性和复杂形成.
- 位点定向突变发生,以确定特定序列基因的作用.
主要成果:
- 诱导性氧化合成酶 (iNOS),S100A8和S100A9的新型异构复合物被确定为一种刺激诱导性S-nitrosylase.
- S100A9作为一个转酶,将NO从iNOS转移到标蛋白.
- 在S100A8和S100A9的协作中,可以直接选择地点,识别保存的I/L-X-C-X2-D/E图案.
- 蛋白质组分析发现了这个iNOS-S100A8/A9复合体的新型蛋白标.
结论:
- iNOS-S100A8/A9复合体代表了依赖刺激的S-化的主要机制.
- 通过特定的序列动图介导的选择性S-化,与蛋白质酸化的机制相似.
- 这一发现为NO信号通路和蛋白质调节提供了新的见解.
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