ArticleJournal of the American Chemical Society2014
Dph7 catalyzes a previously unknown demethylation step in diphthamide biosynthesis.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 30 citations in OpenAlex.
- Manipulation of the cell cycle by HIV-1.Biochemical Society transactions · 2026Review
- Integrative analysis of the role of theTranslational cancer research · 2024Article
- Yeast geneMicrobial cell (Graz, Austria) · 2023Article
- Translational fidelity and growth of Arabidopsis require stress-sensitive diphthamide biosynthesis.Nature communications · 2022Article
- Diphthamide-deficiency syndrome: a novel human developmental disorder and ribosomopathy.European journal of human genetics : EJHG · 2020Article
- Characterization of an l-Ascorbate Catabolic Pathway with Unprecedented Enzymatic Transformations.Journal of the American Chemical Society · 2020Article
- The Crystal Structure of Dph2 in Complex with Elongation Factor 2 Reveals the Structural Basis for the First Step of Diphthamide Biosynthesis.Biochemistry · 2019Article
- The asymmetric function of Dph1-Dph2 heterodimer in diphthamide biosynthesis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Article
- Importance of diphthamide modified EF2 for translational accuracy and competitive cell growth in yeast.PloS one · 2018Article
- A mutated dph3 gene causes sensitivity of Schizosaccharomyces pombe cells to cytotoxic agents.Current genetics · 2017Article
- Elp3 and Dph3 of Schizosaccharomyces pombe mediate cellular stress responses through tRNAScientific reports · 2017Article
- Evolution of the archaeal and mammalian information processing systems: towards an archaeal model for human disease.Cellular and molecular life sciences : CMLS · 2017Review
- Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification.Nature chemical biology · 2016Article
- Hunting Viral Receptors Using Haploid Cells.Annual review of virology · 2015Review
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
Present on archaeal and eukaryotic translation elongation factor 2, diphthamide represents one of the most intriguing post-translational modifications on proteins. The biosynthesis of diphthamide was proposed to occur in three steps requiring seven proteins, Dph1-7, in eukaryotes. The functional assignments of Dph1-5 in the first and second step have been well established. Recent studies suggest that Dph6 (yeast YLR143W or human ATPBD4) and Dph7 (yeast YBR246W or human WDR85) are involved in the last amidation step, with Dph6 being the actual diphthamide synthetase catalyzing the ATP-dependent amidation reaction. However, the exact molecular role of Dph7 is unclear. Here we demonstrate that Dph7 is an enzyme catalyzing a previously unknown step in the diphthamide biosynthesis pathway. This step is between the Dph5- and Dph6-catalyzed reactions. We demonstrate that the Dph5-catalyzed reaction generates methylated diphthine, a previously overlooked intermediate, and Dph7 is a methylesterase that hydrolyzes methylated diphthine to produce diphthine and allows the Dph6-catalyzed amidation reaction to occur. Thus, our study characterizes the molecular function of Dph7 for the first time and provides a revised diphthamide biosynthesis pathway.
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