biostudies-literatureSelvadurai KNIGMS NIH HHS810-2https://www.ebi.ac.uk/biostudies/studies/S-EPMC4479141biostudies-literatureUnknown10(10)Approximately 25% of cytoplasmic tRNAs in eukaryotic organisms have the wobble uridine (U34) modified at C5 through a process that, according to genetic studies, is carried out by the eukaryotic Elongator complex. Here we show that a single archaeal protein, the homolog of the third subunit of the eukaryotic Elongator complex (Elp3), is able to catalyze the same reaction. The mechanism of action by Elp3 described here represents unprecedented chemistry performed on acetyl-CoA.Nature chemical biologyArchaeal Elp3 catalyzes tRNA wobble uridine modification at C5 via a radical mechanism.PMC4479141R01 GM107533GM107533Wang PSeimetz JHuang RHSelvadurai KfalseArchaeal Elp3 catalyzes tRNA wobble uridine modification at C5 via a radical mechanism.Approximately 25% of cytoplasmic tRNAs in eukaryotic organisms have the wobble uridine (U34) modified at C5 through a process that, according to genetic studies, is carried out by the eukaryotic Elongator complex. Here we show that a single archaeal protein, the homolog of the third subunit of the eukaryotic Elongator complex (Elp3), is able to catalyze the same reaction. The mechanism of action by Elp3 described here represents unprecedented chemistry performed on acetyl-CoA.2014-01-01T00:00:00Z2014 Oct2025-04-05T23:17:48.395Z2019-03-27T01:53:59ZS-EPMC44791412515113610.1038/nchembio.1610