The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX.

The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX.
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DOI:
10.3389/fmolb.2017.00097
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发表时间:
2017
影响因子:
5
通讯作者:
Pastore A
Pastore A
中科院分区:
生物学3区
文献类型:
--
作者:
Adinolfi S;Puglisi R;Crack JC;Iannuzzi C;Dal Piaz F;Konarev PV;Svergun DI;Martin S;Le Brun NE;Pastore A

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IscX(或YfhJ)是一种功能未知的蛋白质,参与铁硫簇组装机制,这是一种高度专业化和必需的代谢途径。IscX以低亲和力与铁结合,并与IscS相互作用,IscS是簇组装的核心脱硫酶。先前的研究表明,IscX和CyaY(frataxin的细菌直系同源物)之间存在竞争,以获得相同的IscS结合表面。这种竞争可能表明这两种蛋白质之间存在具有功能意义的联系。使用基于核磁共振,小角散射和生物化学方法的混合方法,我们在这里表明,IscX是CyaY的抑制特性的调制器:通过竞争IscS上的相同位点,IscX的存在拯救了CyaY抑制的酶簇形成的速率。这种影响在低铁浓度下更强,而在高铁浓度下可以忽略不计。这些结果有力地表明了铁作为效应子控制下的铁硫簇组装的双重调节机制。
IscX (or YfhJ) is a protein of unknown function which takes part in the iron-sulfur cluster assembly machinery, a highly specialized and essential metabolic pathway. IscX binds to iron with low affinity and interacts with IscS, the desulfurase central to cluster assembly. Previous studies have suggested a competition between IscX and CyaY, the bacterial ortholog of frataxin, for the same binding surface of IscS. This competition could suggest a link between the two proteins with a functional significance. Using a hybrid approach based on nuclear magnetic resonance, small angle scattering and biochemical methods, we show here that IscX is a modulator of the inhibitory properties of CyaY: by competing for the same site on IscS, the presence of IscX rescues the rates of enzymatic cluster formation which are inhibited by CyaY. The effect is stronger at low iron concentrations, whereas it becomes negligible at high iron concentrations. These results strongly suggest the mechanism of the dual regulation of iron sulfur cluster assembly under the control of iron as the effector.
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