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The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase.


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.

SUBMITTER: Lin TY 

PROVIDER: S-EPMC6367351 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

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The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase.

Lin Ting-Yu TY   Abbassi Nour El Hana NEH   Zakrzewski Karol K   Chramiec-Głąbik Andrzej A   Jemioła-Rzemińska Małgorzata M   Różycki Jan J   Glatt Sebastian S  

Nature communications 20190207 1


The Elongator complex catalyzes posttranscriptional tRNA modifications by attaching carboxy-methyl (cm<sup>5</sup>) 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  ...[more]

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