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Aim32 is a dual-localized 2Fe-2S mitochondrial protein that functions in redox quality control.
Journal of Biological Chemistry ( IF 5.5 ) Pub Date : 2021-08-28 , DOI: 10.1016/j.jbc.2021.101135
Danyun Zhang 1 , Owen R Dailey 2 , Daniel J Simon 2 , Kamilah Roca-Datzer 2 , Yasaman Jami-Alahmadi 3 , Mikayla S Hennen 2 , James A Wohlschlegel 3 , Carla M Koehler 4 , Deepa V Dabir 2
Affiliation  

Yeast is a facultative anaerobe and uses diverse electron acceptors to maintain redox-regulated import of cysteine-rich precursors via the mitochondrial intermembrane space assembly (MIA) pathway. With the growing diversity of substrates utilizing the MIA pathway, understanding the capacity of the intermembrane space (IMS) to handle different types of stress is crucial. We used MS to identify additional proteins that interacted with the sulfhydryl oxidase Erv1 of the MIA pathway. Altered inheritance of mitochondria 32 (Aim32), a thioredoxin-like [2Fe-2S] ferredoxin protein, was identified as an Erv1-binding protein. Detailed localization studies showed that Aim32 resided in both the mitochondrial matrix and IMS. Aim32 interacted with additional proteins including redox protein Osm1 and protein import components Tim17, Tim23, and Tim22. Deletion of Aim32 or mutation of conserved cysteine residues that coordinate the Fe-S center in Aim32 resulted in an increased accumulation of proteins with aberrant disulfide linkages. In addition, the steady-state level of assembled TIM22, TIM23, and Oxa1 protein import complexes was decreased. Aim32 also bound to several mitochondrial proteins under nonreducing conditions, suggesting a function in maintaining the redox status of proteins by potentially targeting cysteine residues that may be sensitive to oxidation. Finally, Aim32 was essential for growth in conditions of stress such as elevated temperature and hydroxyurea, and under anaerobic conditions. These studies suggest that the Fe-S protein Aim32 has a potential role in general redox homeostasis in the matrix and IMS. Thus, Aim32 may be poised as a sensor or regulator in quality control for a broad range of mitochondrial proteins.

中文翻译:

Aim32 是一种双定位 2Fe-2S 线粒体蛋白,在氧化还原质量控制中起作用。

酵母是一种兼性厌氧菌,它使用多种电子受体通过线粒体膜间空间组装 (MIA) 途径维持氧化还原调节的富含半胱氨酸前体的输入。随着利用 MIA 途径的底物日益多样化,了解膜间空间 (IMS) 处理不同类型压力的能力至关重要。我们使用 MS 来鉴定与 MIA 途径的巯基氧化酶 Erv1 相互作用的其他蛋白质。线粒体 32 (Aim32) 的遗传改变,一种硫氧还蛋白样 [2Fe-2S] 铁氧还蛋白蛋白,被鉴定为 Erv1 结合蛋白。详细的定位研究表明,Aim32 存在于线粒体基质和 IMS 中。Aim32 与其他蛋白质相互作用,包括氧化还原蛋白 Osm1 和蛋白质输入成分 Tim17、Tim23 和 Tim22。Aim32 的缺失或与 Aim32 中的 Fe-S 中心协调的保守半胱氨酸残基的突变导致具有异常二硫键的蛋白质的积累增加。此外,组装的 TIM22、TIM23 和 Oxa1 蛋白输入复合物的稳态水平降低。Aim32 还在非还原条件下与几种线粒体蛋白结合,表明通过潜在地靶向可能对氧化敏感的半胱氨酸残基来维持蛋白质的氧化还原状态的功能。最后,Aim32 对于在高温和羟基脲等压力条件下以及厌氧条件下的生长至关重要。这些研究表明,Fe-S 蛋白 Aim32 在基质和 IMS 中的一般氧化还原稳态中具有潜在作用。因此,
更新日期:2021-08-27
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