期刊
EMBO REPORTS
卷 8, 期 2, 页码 194-199出版社
WILEY
DOI: 10.1038/sj.embor.7400881
关键词
acidic ridge; Fe-S cluster; frataxin; Isu1; mitochondria; acidic residue
资金
- Medical Research Council [MC_U117584256] Funding Source: researchfish
- MRC [MC_U117584256] Funding Source: UKRI
- Medical Research Council [MC_U117584256] Funding Source: Medline
Friedreich ataxia is caused by decreased levels of frataxin, a mitochondrial acidic protein that is assumed to act as chaperone in the assembly of Fe-S clusters on the scaffold Isu protein. Frataxin has the in vitro capacity to form iron-loaded multimers, which also suggests an iron storage function. It has been reported that alanine substitution of residues in an acidic ridge of yeast frataxin (Yfh1) elicits loss of iron binding in vitro but has no effect on Fe-S cluster synthesis in vivo. Here, we show that a marked change in the electrostatic properties of a specific region of Yfh1 surface-by substituting two or four acidic residues by lysine or alanine, respectively-impairs Fe-S cluster assembly, weakens the interaction between Yfh1 and Isu1, and increases oxidative damage. Therefore, the acidic ridge is essential for the Yfhl function and is likely to be involved in iron-mediated protein-protein interactions.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据