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Mammalian iron-sulfur cluster biogenesis: Recent insights into the roles of frataxin, acyl carrier protein and ATPase-mediated transfer to recipient proteins.
Current opinion in chemical biology Pub Date : 2020-01-06 , DOI: 10.1016/j.cbpa.2019.11.014
Nunziata Maio 1 , Anshika Jain 1 , Tracey A Rouault 1
Affiliation  

The recently solved crystal structures of the human cysteine desulfurase NFS1, in complex with the LYR protein ISD11, the acyl carrier protein ACP, and the main scaffold ISCU, have shed light on the molecular interactions that govern initial cluster assembly on ISCU. Here, we aim to highlight recent insights into iron-sulfur (Fe-S) cluster (ISC) biogenesis in mammalian cells that have arisen from the crystal structures of the core ISC assembly complex. We will also discuss how ISCs are delivered to recipient proteins and the challenges that remain in dissecting the pathways that deliver clusters to numerous Fe-S recipient proteins in both the mitochondrial matrix and cytosolic compartments of mammalian cells.

中文翻译:


哺乳动物铁硫簇生物合成:对 frataxin、酰基载体蛋白和 ATP 酶介导的受体蛋白转移作用的最新见解。



最近解决的人半胱氨酸脱硫酶 NFS1 的晶体结构,与 LYR 蛋白 ISD11、酰基载体蛋白 ACP 和主要支架 ISCU 的复合物,揭示了控制 ISCU 上初始簇组装的分子相互作用。在这里,我们的目的是强调对哺乳动物细胞中铁硫(Fe-S)簇(ISC)生物合成的最新见解,这些生物合成是由核心 ISC 组装复合物的晶体结构产生的。我们还将讨论 ISC 如何传递至受体蛋白,以及剖析将簇传递至哺乳动物细胞线粒体基质和胞质室中众多 Fe-S 受体蛋白的途径仍然面临的挑战。
更新日期:2020-01-06
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