Chaperone activity with a redox switch
Chaperone activity with a redox switch
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DOI：
10.1016/s0092-8674(00)80547-4
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发表时间：
1999-02-05
期刊：
影响因子：
64.5
通讯作者：
Bardwell, JCA
中科院分区：
文献类型：
--
作者：
Jakob, U;Muse, W;Bardwell, JCA
Hsp33 是新发现的愈合休克蛋白家族的成员，被发现是一种非常有效的分子伴侣。 Hsp33 与所有其他已知分子伴侣的区别在于其功能调节模式。其活性受氧化还原调节，Hsp33 是一种细胞质定位蛋白，具有高反应性半胱氨酸，可对氧化还原环境的变化做出快速反应。 H2O2 等氧化条件会导致 Hsp33 中形成二硫键，这一过程会激活其伴侣功能。体外和体内实验表明，Hsp33 可以保护细胞免受氧化剂的侵害，这使我们得出这样的结论：我们发现了一个在细菌氧化应激防御系统中发挥重要作用的蛋白质家族。
Hsp33, a member of a newly discovered heal shock protein family, was found to be a very potent molecular chaperone. Hsp33 is distinguished from all other known molecular chaperones by its mode of functional regulation. Its activity is redox regulated, Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function. In vitro and in vivo experiments suggest that Hsp33 protects cells from oxidants, leading us to conclude that we have found a protein family that plays an important role in the bacterial defense system toward oxidative stress.