Lin Zhewang, Dong Min, Zhang Yugang, Lee Eunyoung Alisa, Lin Hening
Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Nat Chem Biol. 2016 Dec;12(12):995-997. doi: 10.1038/nchembio.2190. Epub 2016 Oct 3.
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 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.
白喉酰胺和tRNA摆动尿苷修饰都需要白喉酰胺生物合成3（Dph3）蛋白作为其生物合成酶中铁硫簇的电子供体。在这里，我们使用蛋白质组学方法，将酿酒酵母细胞色素b还原酶（Cbr1）鉴定为Dph3的NADH依赖性还原酶。Dph3的NADH和Cbr1依赖性还原可能在细胞代谢状态和蛋白质翻译之间提供一种调节联系。
