A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation
A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation
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DOI：
10.1016/s0092-8674(02)01048-6
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发表时间：
2002-11-15
期刊：
影响因子：
64.5
通讯作者：
Toledano, MB
中科院分区：
文献类型：
--
作者：
Delaunay, A;Pflieger, D;Toledano, MB
Yap1转录因子调控酿酒酵母过氧化氢稳态。当过氧化氢水平增加时，Yap1被氧化激活。我们发现Yap1不被过氧化氢直接氧化。我们发现谷胱甘肽过氧化物酶（GPX）样酶Gpx3是该途径的第二个组成部分，起着过氧化氢信号到Yap1的传感器和传感器的作用。当被H2O2氧化时，Gpx3 Cys36通过二硫键桥接Yap1 Cys598。这个分子间二硫键随后被分解成Yap1分子内二硫键，这是调节因子的激活形式。硫氧还蛋白通过减少传感器和调节器来关闭这一途径。这些数据揭示了gpx样酶的氧化还原信号功能，并阐明了真核生物的氢过氧化物感应机制。因此Gpx3是氢过氧化物受体和氧化还原传感器。
The Yap1 transcription factor regulates hydroperoxide homeostasis in S. cerevisiae. Yap1 is activated by oxidation when hydroperoxide levels increase. We show that Yap1 is not directly oxidized by hydroperoxide. We identified the glutathione peroxidase (GPX)-like enzyme Gpx3 as a second component of the pathway, serving the role of sensor and transducer of the hydroperoxide signal to Yap1. When oxidized by H2O2, Gpx3 Cys36 bridges Yap1 Cys598 by a disulfide bond. This intermolecular disulfide bond is then resolved into a Yap1 intramolecular disulfide bond, the activated form of the regulator. Thioredoxin turns off the pathway by reducing both sensor and regulator. These data reveal a redox-signaling function for a GPx-like enzyme and elucidate a eukaryotic hydroperoxide-sensing mechanism. Gpx3 is thus a hydroperoxide receptor and redox-transducer.