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

Pub. Date : 2016 Dec

PMID : 27694803






8 Functional Relationships(s)
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Protein Name
Organism
1 Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification. Uridine diphthamide biosynthesis 3 Homo sapiens
2 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. diphthamide diphthamide biosynthesis 3 Homo sapiens
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. Uridine diphthamide biosynthesis 3 Homo sapiens
4 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. diphthamide diphthamide biosynthesis 3 Homo sapiens
5 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. Iron diphthamide biosynthesis 3 Homo sapiens
6 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. Sulfur diphthamide biosynthesis 3 Homo sapiens
7 Here, using a proteomic approach, we identified Saccharomyces cerevisiae cytochrome b5 reductase (Cbr1) as a NADH-dependent reductase for Dph3. NAD diphthamide biosynthesis 3 Homo sapiens
8 The NADH- and Cbr1-dependent reduction of Dph3 may provide a regulatory linkage between cellular metabolic state and protein translation. NAD diphthamide biosynthesis 3 Homo sapiens