Archaeal Elp3 catalyzes tRNA wobble uridine modification at C5 via a radical mechanism

August 24th, 2014 by Kiruthika Selvadurai

Nature Chemical Biology 10, 810 (2014). doi:10.1038/nchembio.1610

Authors: Kiruthika Selvadurai, Pei Wang, Joseph Seimetz & Raven H Huang

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.

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