Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification.
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 b5reductase (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.
Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Zhewang
http://orcid.org/0000-0003-1301-6661
Z
Lin
Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Min
M
Dong
Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Yugang
Y
Zhang
Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Eunyoung Alisa
EA
Lee
Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Hening
http://orcid.org/0000-0002-0255-2701
H
Lin
D042966:Cytochrome-B(5) Reductase / Q000378:metabolism*; D012343:RNA, Transfer / Q000378:metabolism*; D012097:Repressor Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D014529:Uridine / Q000378:metabolism*
C459979:KTI11 protein, S cerevisiae; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D012343:RNA, Transfer; D042966:Cytochrome-B(5) Reductase; D014529:Uridine
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