The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase

Ting-Yu Lin, Nour El Hana Abbassi, Karol Zakrzewski, Andrzej Chramiec-Głąbik, Małgorzata Jemioła-Rzemińska, Jan Różycki and Sebastian Glatt ()
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Ting-Yu Lin: Jagiellonian University
Nour El Hana Abbassi: Jagiellonian University
Karol Zakrzewski: Jagiellonian University
Andrzej Chramiec-Głąbik: Jagiellonian University
Małgorzata Jemioła-Rzemińska: Jagiellonian University
Jan Różycki: Jagiellonian University
Sebastian Glatt: Jagiellonian University

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-08579-2

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