Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification

October 3rd, 2016 by Zhewang Lin

Nature Chemical Biology 12, 995 (2016). doi:10.1038/nchembio.2190

Authors: Zhewang Lin, Min Dong, Yugang Zhang, Eunyoung Alisa Lee & Hening Lin

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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