Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification. Academic Article uri icon

Overview

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.

publication date

  • October 3, 2016

Research

keywords

  • Cytochrome-B(5) Reductase
  • RNA, Transfer
  • Repressor Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Uridine

Identity

PubMed Central ID

  • PMC5110365

Scopus Document Identifier

  • 84989954716

Digital Object Identifier (DOI)

  • 10.1038/nchembio.2190

PubMed ID

  • 27694803

Additional Document Info

volume

  • 12

issue

  • 12