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
中科院分区:
文献类型:
--
作者:
Chahal, Harsimranjit K.;Dai, Yuyuan;Saini, Avneesh;Ayala-Castro, Carla;Outten, F. Wayne
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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