Skip to Main content Skip to Navigation
Journal articles

Structural basis for tRNA modification by Elp3 from Dehalococcoides mccartyi

Abstract : During translation elongation, decoding is based on the recognition of codons by corresponding tRNA anticodon triplets. Molecular mechanisms that regulate global protein synthesis via specific base modifications in tRNA anticodons are receiving increasing attention. The conserved eukaryotic Elongator complex specifically modifies uridines located in the wobble base position of tRNAs. Mutations in Elongator subunits are associated with certain neurodegenerative diseases and cancer. Here we present the crystal structure of D. mccartyi Elp3 (DmcElp3) at 2.15-Å resolution. Our results reveal an unexpected arrangement of Elp3 lysine acetyltransferase (KAT) and radical S-adenosyl methionine (SAM) domains, which share a large interface and form a composite active site and tRNA-binding pocket, with an iron–sulfur cluster located in the dimerization interface of two DmcElp3 molecules. Structure-guided mutagenesis studies of yeast Elp3 confirmed the relevance of our findings for eukaryotic Elp3s and should aid in understanding the cellular functions and pathophysiological roles of Elongator.
Document type :
Journal articles
Complete list of metadatas

https://hal.archives-ouvertes.fr/hal-01413474
Contributor : Laure Azzopardi <>
Submitted on : Friday, December 9, 2016 - 6:12:19 PM
Last modification on : Wednesday, May 6, 2020 - 5:10:07 PM

Links full text

Identifiers

Collections

Citation

Sebastian Glatt, Rene Zabel, Olga Kolaj-Robin, Osita Onuma, Florence Baudin, et al.. Structural basis for tRNA modification by Elp3 from Dehalococcoides mccartyi. Nature Structural and Molecular Biology, Nature Publishing Group, 2016, pp.794-802. ⟨10.1038/nsmb.3265⟩. ⟨hal-01413474⟩

Share

Metrics

Record views

666