Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification
Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification
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DOI：
10.1038/nchembio.2190
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发表时间：
2016-12-01
影响因子：
14.8
通讯作者：
Lin, Hening
中科院分区：
文献类型：
--
作者：
Lin, Zhewang;Dong, Min;Lin, Hening
二苯二甲酰胺和tRNA摆动尿苷修饰都需要二苯二甲酰胺生物合成3（Dph3）蛋白作为其生物合成酶中铁硫簇的电子供体。在这里，使用蛋白质组学方法，我们确定了酿酒酵母细胞色素B（5）还原酶（Cbr 1）作为NADPH依赖性还原酶的Dph 3。依赖于NADH和Cbr 1的Dph 3还原可能在细胞代谢状态和蛋白质翻译之间提供调节联系。
Diphthamide and the tRNA wobble uridine modifications both require diphthamide biosynthesis 3 (Dph3) protein as an electron donor for the iron-sulfur clusters in their biosynthetic enzymes. Here, using a proteomic approach, we identified Saccharomyces cerevisiae cytochrome b(5) reductase (Cbr1) as a NADH-dependent reductase for Dph3. The NADH-and Cbr1-dependent reduction of Dph3 may provide a regulatory linkage between cellular metabolic state and protein translation.