Arabidopsis cytosolic Nbp35 homodimer can assemble both [2Fe-2S] and [4Fe-4S] clusters in two distinct domains
Arabidopsis cytosolic Nbp35 homodimer can assemble both [2Fe-2S] and [4Fe-4S] clusters in two distinct domains
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DOI：
10.1016/j.bbrc.2008.11.138
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发表时间：
2009-01-23
影响因子：
3.1
通讯作者：
Nakai, Masato
中科院分区：
文献类型：
--
作者：
Kohbushi, Hirokazu;Nakai, Yumi;Nakai, Masato
铁硫蛋白在真核生物的多种代谢过程中起着重要的生理作用。在植物中，铁硫簇生物合成已知发生在线粒体和叶绿体中。然而，到目前为止，还没有鉴定出介导植物细胞胞质中铁硫簇递送的组分。在这里，我们报告的细胞溶质Nbp 35同源命名AtNbp 35拟南芥的鉴定和表征。AtNbp 35缺陷拟南芥突变体是幼苗致死的。与先前表征的与ScCfd 1形成异源四聚体的酵母ScNbp 35不同，AtNbp 35在胞质溶胶中形成同源二聚体，并且可以分别在其氨基和羧基末端结构域上携带[4Fe-4S]和[2Fe-2S]簇。两者合计，我们的数据表明，Nbp 35在铁硫簇组装和传递在植物细胞胞质溶胶作为一个双功能分子支架中起着关键作用。(C)2008年爱思唯尔公司All rights reserved.
Iron-sulfur proteins play physiologically important roles in a variety of metabolic processes in eukaryotes. In plants, iron-sulfur cluster biosynthesis is known to take place both in mitochondria and chloroplasts. However no components that mediate iron-sulfur cluster delivery in the plant cell cytosol have been identified so far. Here we report identification and characterization of a cytosolic Nbp35 homolog named AtNbp35 from Arabidopsis thaliana. AtNbp35-deficient Arabidopsis mutants were seedling lethal. Unlike the previously characterized yeast ScNbp35 which forms a heterotetramer with ScCfd1, AtNbp35 forms a homodimer in the cytosol and can harbor both [4Fe-4S] and [2Fe-2S] clusters on its amino- and carboxyl-terminal domains, respectively. Taken together, our data suggest that Nbp35 plays a pivotal role in iron-sulfur cluster assembly and delivery in the plant cell cytosol as a bifunctional molecular scaffold. (C) 2008 Elsevier Inc. All rights reserved.