The SufBCD Fe-S scaffold complex interacts with SufA for Fe-S cluster transfer.

The SufBCD Fe-S scaffold complex interacts with SufA for Fe-S cluster transfer.
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DOI:
10.1021/bi901518y
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发表时间:
2009-11-10
期刊:
影响因子:
2.9
通讯作者:
Outten, F. Wayne
Outten, F. Wayne
中科院分区:
生物学3区
文献类型:
--
作者:
Chahal, Harsimranjit K.;Dai, Yuyuan;Saini, Avneesh;Ayala-Castro, Carla;Outten, F. Wayne

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铁-硫团簇是从固氮到呼吸等生物途径中的关键铁辅助因子。由于亚铁和硫化物对细胞的毒性,体内Fe-S簇的组装是通过多蛋白质生物合成途径进行的。铁-S簇组装蛋白运输铁和硫化物,组装新生的铁-S簇,并在体内正确地将铁-S簇转移到合适的靶金属蛋白上。革兰氏阴性杆菌大肠杆菌含有一个应激反应的铁-S簇组装系统,即SufABCDSE途径,该途径在铁饥饿和氧化应激条件下发挥作用,破坏铁-S的动态平衡。结合蛋白质相互作用和体外Fe-S簇组装实验,我们研究了SufBCD复合体和SuFa蛋白在Suf Fe-S簇生物合成过程中的相对作用。这些研究表明,SuFA与SufBCD相互作用,以接受在SufBCD络合物上从头形成的Fe-S团簇。我们的结果首次提供了生化证据表明,Suf途径中的SufBCD复合体作为一种新型的Fe-S支架系统,组装新生的簇并将它们转移到Sufa Fe-S航天飞机上。
Iron-sulfur clusters are key iron cofactors in biological pathways ranging from nitrogen fixation to respiration. Due to the toxicity of ferrous iron and sulfide to the cell, in vivo Fe-S cluster assembly is carried out by multi-protein biosynthetic pathways. Fe-S cluster assembly proteins traffic iron and sulfide, assemble nascent Fe-S clusters, and correctly transfer Fe-S clusters to the appropriate target metalloproteins in vivo. The gram-negative bacterium E. coli contains a stress-responsive Fe-S cluster assembly system, the SufABCDSE pathway, that functions under iron starvation and oxidative stress conditions that compromise Fe-S homeostasis. Using a combination of protein-protein interaction and in vitro Fe-S cluster assembly assays, we have characterized the relative roles of the SufBCD complex and the SufA protein during Suf Fe-S cluster biosynthesis. These studies reveal that SufA interacts with SufBCD in order to accept Fe-S clusters formed de novo on the SufBCD complex. Our results represent the first biochemical evidence that the SufBCD complex within the Suf pathway functions as a novel Fe-S scaffold system to assemble nascent clusters and transfer them to the SufA Fe-S shuttle.
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