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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

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

Lin Zhewang Z Dong Min M Zhang Yugang Y Lee Eunyoung Alisa EA Lin Hening H

Nature chemical biology 20161003 12

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<sub>5</sub> 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. ...[more]

PMID: 27694803

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