An Intrinsically Disordered Domain Has a Dual Function Coupled to Compartment-Dependent Redox Control
An Intrinsically Disordered Domain Has a Dual Function Coupled to Compartment-Dependent Redox Control
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DOI：
10.1016/j.jmb.2012.11.032
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发表时间：
2013-02-08
影响因子：
5.6
通讯作者：
Tokatlidis, Kostas
中科院分区：
文献类型：
--
作者：
Banci, Lucia;Bertini, Ivano;Tokatlidis, Kostas
非结构化蛋白质结构域的功能作用是本质上无序蛋白质框架中的一个新兴领域。迄今为止，内在无序结构域（IDD）参与线粒体蛋白质靶向和生物发生过程尚不清楚。在这里，我们表征了位于线粒体膜间隙的巯基氧化酶 ALR（肝再生增强剂）的 IDD 的结构/动态和功能特性。与几种本质上无序的蛋白质的展开到折叠的结构转变不同，底物识别事件和其穿梭半胱氨酸对的氧化还原开关都与任何此类结构变化无关。然而，这个非结构化结构域在两个细胞区室中发挥双重功能：它（i）作为细胞质中的线粒体靶向信号，（ii）作为膜间空间二硫键中继系统中的关键识别位点。该结构域为 IDD 提供了一个令人兴奋的新范例，确保了与细胞内细胞器靶向相关的两种不同功能。 (C) 2012 Elsevier Ltd. 保留所有权利。
The functional role of unstructured protein domains is an emerging field in the frame of intrinsically disordered proteins. The involvement of intrinsically disordered domains (IDDs) in protein targeting and biogenesis processes in mitochondria is so far not known. Here, we have characterized the structural/dynamic and functional properties of an IDD of the sulfhydryl oxidase ALR (augmenter of liver regeneration) located in the intermembrane space of mitochondria. At variance to the unfolded-to-folded structural transition of several intrinsically disordered proteins, neither substrate recognition events nor redox switch of its shuttle cysteine pair is linked to any such structural change. However, this unstructured domain performs a dual function in two cellular compartments: it acts (i) as a mitochondrial targeting signal in the cytosol and (ii) as a crucial recognition site in the disulfide relay system of intermembrane space. This domain provides an exciting new paradigm for IDDs ensuring two distinct functions that are linked to intracellular organelle targeting. (C) 2012 Elsevier Ltd. All rights reserved.