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首页> 外文期刊>Journal of Molecular Biology >Characterization of Mitochondrial YME1L Protease Oxidative Stress-Induced Conformational State
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Characterization of Mitochondrial YME1L Protease Oxidative Stress-Induced Conformational State

机译:线粒体YME1L蛋白酶氧化应激诱导的构象状态的表征

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Oxidative stress is a common challenge to mitochondrial function where reactive oxygen species are capable of significant organelle damage. The generation of mitochondrial reactive oxygen species occurs in the inner membrane and matrix compartments as a consequence of subunit function in the electron transport chain and citric acid cycle, respectively. Maintenance of mitochondrial proteostasis and stress response is facilitated by compartmentalized proteases that couple the energy of ATP hydrolysis to unfolding and the regulated removal of damaged, misfolded, or aggregated proteins. The mitochondrial protease YME1L functions in the maintenance of proteostasis in the intermembrane space. YME1L is an inner membrane-anchored hexameric protease with distinct N-terminal, transmembrane, AAA+ (ATPases associated with various cellular activities), and C-terminal M41 zinc-dependent protease domains.
机译:氧化应激是对线粒体功能的常见挑战,其中活性氧物质能够显着有细胞石损伤。 由于电子传输链和柠檬酸循环分别发生在内膜和基质隔室中的线粒体反应性氧物质的产生。 通过划分的蛋白酶促进了线粒体蛋白质和应激反应的维持,该蛋白酶促进了ATP水解能量与展开的能量,并受到受损,错误的或聚集蛋白的调节去除。 线粒体蛋白酶YME1L在膜间空间中维持蛋白质的作用。 YME1L是一种内膜锚定的六聚体蛋白酶,具有不同的N-末端,跨膜,AAA +(与各种细胞活性相关的ATP酶),以及C末端M41锌依赖性蛋白酶结构域。

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