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

ABSTRACT: 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.

SUBMITTER: Lin Z 

PROVIDER: S-EPMC5110365 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature