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用于GroEL/ES基板的氧化还原质量控制的分子装置

Emile Dupuy¹, Sander Egbert Van der Verren², Jiusheng Lin³

¹WELBIO, Avenue Hippocrate 75, 1200 Brussels, Belgium; de Duve Institute, Université catholique de Louvain, Avenue Hippocrate 75, 1200 Brussels, Belgium.

|February 10, 2023

概括

像Hsp60 (热冲击蛋白60) 和它们的Hsp10辅因子这样的分子伴侣对蛋白质折叠至关重要. 这项研究揭示了一种新的蛋白质,CnoX,作为Hsp60护理GroEL的氧化还原质量控制插件.

科学领域:

分子生物学
蛋白质折叠
结构生物学

背景情况:

在所有细胞中,hsp60护理素和hsp10辅助因子对于蛋白质折叠至关重要,作为关键的分子护理素.
尽管进行了广泛的研究,但 chaperonins 促进蛋白质折叠的确切机制仍然不完全理解.

研究的目的:

调查细菌Hsp60护理剂GroEL与一种新型蛋白质CnoX之间的相互作用.
阐明GroEL-CnoX复合体在蛋白质折叠和质量控制中的结构基础和功能影响.

主要方法:

在GroEL和CnoX之间进行复杂形成分析.
用冷电子显微镜 (Cryo-EM) 来确定GroEL-CnoX复合物的结构.
在CnoX,GroEL和GroEL基底之间识别混合二硫化物复合物.

主要成果:

GroEL与CnoX形成一个稳定的复合体,该蛋白质具有伴侣和氧化还原功能.
通过保留的C端α螺旋,CnoX与GroEL结合在外部,远离基质结合部位.
CnoX作为氧化还原质量控制插件,与GroEL基质形成混合二硫化物,并在GroES结合时释放.

结论:

在GroEL chaperonin系统中,CnoX作为一种新型的氧化还原活性辅助因子.
这种相互作用突出显示了Hsp60分子插件的保存机制,而CnoX类蛋白质可能存在于真核生物中.
这一发现扩大了我们对伴侣辅助蛋白质折叠和细胞质量控制机制的理解.

关键词:

美国陪伴者陪伴者蛋白质折叠蛋白质稳定性氧化还原氨酸

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