Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification.
Nat. Chem. Biol.2016 Dec;12(12):995-997. Epub 2016 Oct 03
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摘要
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 b5 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.
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基因功能
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原始数据
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文献解读
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