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Defining the mechanism of the mitochondrial Atm1p [2Fe-2S] cluster exporter.
Metallomics ( IF 2.9 ) Pub Date : 2020-04-09 , DOI: 10.1039/c9mt00286c
Stephen A Pearson 1 , Christine Wachnowsky 2 , J A Cowan 3
Affiliation  

Iron–sulfur cluster proteins play key roles in a multitude of physiological processes; including gene expression, nitrogen and oxygen sensing, electron transfer, and DNA repair. Biosynthesis of iron–sulfur clusters occurs in mitochondria on iron–sulfur cluster scaffold proteins in the form of [2Fe–2S] cores that are then transferred to apo targets within metabolic or respiratory pathways. The mechanism by which cytosolic Fe–S cluster proteins mature to their holo forms remains controversial. The mitochondrial inner membrane protein Atm1p can transport glutathione-coordinated iron–sulfur clusters, which may connect the mitochondrial and cytosolic iron–sulfur cluster assembly systems. Herein we describe experiments on the yeast Atm1p/ABCB7 exporter that provide additional support for a glutathione-complexed cluster as the natural physiological substrate and a reflection of the endosymbiotic model of mitochondrial evolution. These studies provide insight on the mechanism of cluster transport and the molecular basis of human disease conditions related to ABCB7. Recruitment of MgATP following cluster binding promotes a structural transition from closed to open conformations that is mediated by coupling helices, with MgATP hydrolysis facilitating the return to the closed state.

中文翻译:

定义线粒体 Atm1p [2Fe-2S] 簇输出器的机制。

铁硫簇蛋白在多种生理过程中起着关键作用;包括基因表达、氮氧传感、电子转移和 DNA 修复。铁硫簇的生物合成发生在铁硫簇支架蛋白的线粒体中,以 [2Fe-2S] 核心的形式,然后转移到代谢或呼吸途径中的载脂蛋白靶标。胞质 Fe-S 簇蛋白成熟为其全息形式的机制仍存在争议。线粒体内膜蛋白 Atm1p 可以运输谷胱甘肽配位的铁硫簇,这可能连接线粒体和胞质铁硫簇组装系统。在这里,我们描述了酵母 Atm1p/ABCB7 出口蛋白的实验,这些实验为作为天然生理底物的谷胱甘肽复合簇提供了额外的支持,并反映了线粒体进化的内共生模型。这些研究提供了对簇运输机制和与 ABCB7 相关的人类疾病状况的分子基础的深入了解。簇结合后 MgATP 的募集促进了由耦合螺旋介导的从封闭构象到开放构象的结构转变,MgATP 水解促进返回封闭状态。
更新日期:2020-04-09
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