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Schizosaccharomyces pombe Grx4 regulates the transcriptional repressor Php4 via [2Fe–2S] cluster binding
Metallomics ( IF 2.9 ) Pub Date : 2017-07-12 00:00:00 , DOI: 10.1039/c7mt00144d
Adrienne C. Dlouhy 1, 2, 3, 4 , Jude Beaudoin 5, 6, 7, 8, 9 , Simon Labbé 5, 6, 7, 8, 9 , Caryn E. Outten 1, 2, 3, 4
Affiliation  

The fission yeast Schizosaccharomyces pombe expresses the CCAAT-binding factor Php4 in response to iron deprivation. Php4 forms a transcription complex with Php2, Php3, and Php5 to repress the expression of iron proteins as a means to economize iron usage. Previous in vivo results demonstrate that the function and location of Php4 are regulated in an iron-dependent manner by the cytosolic CGFS type glutaredoxin Grx4. In this study, we aimed to biochemically define these protein–protein and protein–metal interactions. Grx4 was found to bind a [2Fe–2S] cluster with spectroscopic features similar to other CGFS glutaredoxins. Grx4 and Php4 also copurify as a complex with a [2Fe–2S] cluster that is spectroscopically distinct from the cluster on Grx4 alone. In vitro titration experiments suggest that these Fe–S complexes may not be interconvertible in the absence of additional factors. Furthermore, conserved cysteines in Grx4 (Cys172) and Php4 (Cys221 and Cys227) are necessary for Fe–S cluster binding and stable complex formation. Together, these results show that Grx4 controls Php4 function through binding of a bridging [2Fe–2S] cluster.

中文翻译:

粟酒裂殖酵母Grx4通过[2Fe–2S]簇结合调节转录阻遏物Php4

裂变酵母粟酒裂殖酵母响应铁缺乏而表达CCAAT结合因子Php4。Php4与Php2,Php3和Php5形成转录复合物,以抑制铁蛋白的表达,从而节省了铁的使用。先前的体内结果表明,Php4的功能和位置受细胞溶质CGFS型谷胱甘肽Grx4以铁依赖性方式调节。在这项研究中,我们旨在生化地定义这些蛋白质-蛋白质和蛋白质-金属相互作用。发现Grx4结合了[2Fe–2S]簇,并具有类似于其他CGFS戊二醛毒素的光谱特征。Grx4和Php4还可以与[2Fe–2S]团簇复合纯化,该团簇在光谱学上不同于单独的Grx4团簇。体外滴定实验表明,在没有其他因素的情况下,这些Fe–S络合物可能无法相互转化。此外,Grx4(Cys172)和Php4(Cys221和Cys227)中的保守半胱氨酸对于Fe–S团簇结合和稳定的复合物形成是必需的。总之,这些结果表明,Grx4通过桥接[2Fe–2S]簇的结合来控制Php4的功能。
更新日期:2017-08-03
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