Literature DB >> 25151136

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

Kiruthika Selvadurai1, Pei Wang1, Joseph Seimetz1, Raven H Huang1.   

Abstract

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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Year:  2014        PMID： 25151136      PMCID： PMC4479141          DOI： 10.1038/nchembio.1610

Source DB:  PubMed          Journal:  Nat Chem Biol        ISSN： 1552-4450            Impact factor:   15.040


  23 in total

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5.  Post-transcriptional modification in archaeal tRNAs: identities and phylogenetic relations of nucleotides from mesophilic and hyperthermophilic Methanococcales.

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Review 10.  Structural insights into the function of Elongator.

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