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

Diphthamide and the tRNA wobble uridine modifications both require Dph3 (DiPHthamide biosynthesis 3) 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(5) reductase (Cbr1) as a...

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Detalles Bibliográficos
Autores principales: Lin, Zhewang, Dong, Min, Zhang, Yugang, Lee, Eunyoung Alisa, Lin, Hening
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5110365/
https://www.ncbi.nlm.nih.gov/pubmed/27694803
http://dx.doi.org/10.1038/nchembio.2190
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author Lin, Zhewang
Dong, Min
Zhang, Yugang
Lee, Eunyoung Alisa
Lin, Hening
author_facet Lin, Zhewang
Dong, Min
Zhang, Yugang
Lee, Eunyoung Alisa
Lin, Hening
author_sort Lin, Zhewang
collection PubMed
description Diphthamide and the tRNA wobble uridine modifications both require Dph3 (DiPHthamide biosynthesis 3) 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(5) 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.
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spelling pubmed-51103652017-04-03 Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification Lin, Zhewang Dong, Min Zhang, Yugang Lee, Eunyoung Alisa Lin, Hening Nat Chem Biol Article Diphthamide and the tRNA wobble uridine modifications both require Dph3 (DiPHthamide biosynthesis 3) 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(5) 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. 2016-10-03 2016-12 /pmc/articles/PMC5110365/ /pubmed/27694803 http://dx.doi.org/10.1038/nchembio.2190 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Lin, Zhewang
Dong, Min
Zhang, Yugang
Lee, Eunyoung Alisa
Lin, Hening
Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification
title Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification
title_full Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification
title_fullStr Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification
title_full_unstemmed Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification
title_short Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification
title_sort cbr1 is a dph3 reductase required for the trna wobble uridine modification
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5110365/
https://www.ncbi.nlm.nih.gov/pubmed/27694803
http://dx.doi.org/10.1038/nchembio.2190
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