The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Ting-Yu Lin, Nour El Hana Abbassi, Karol Zakrzewski, Andrzej Chramiec-Głąbik, Małgorzata Jemioła-Rzemińska, Jan Różycki, Sebastian Glatt

ABSTRACT

The Elongator complex catalyzes posttranscriptional tRNA modifications by attaching carboxy-methyl (cm5) moieties to uridine bases located in the wobble position. The catalytic subunit Elp3 is highly conserved and harbors two individual subdomains, a radical S-adenosyl methionine (rSAM) and a lysine acetyltransferase (KAT) domain. The details of its modification reaction cycle and particularly the substrate specificity of its KAT domain remain elusive. Here, we present the co-crystal structure of bacterial Elp3 (DmcElp3) bound to an acetyl-CoA analog and compare it to the structure of a monomeric archaeal Elp3 from Methanocaldococcus infernus (MinElp3). Furthermore, we identify crucial active site residues, confirm the importance of the extended N-terminus for substrate recognition and uncover the specific induction of acetyl-CoA hydrolysis by different tRNA species. In summary, our results establish the clinically relevant Elongator subunit as a non-canonical acetyltransferase and genuine tRNA modification enzyme. More... »

PAGES

625

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-019-08579-2

DOI

http://dx.doi.org/10.1038/s41467-019-08579-2

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1111977297

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30733442


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