The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase
| Autor: | M. Jemiola-Rzeminska, Sebastian Glatt, N.E.H. Abbassi, A. Chramiec-Glabik, K. Zakrzewski, Ting-Yu Lin, J. Rozycki |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
TRNA modification Saccharomyces cerevisiae Proteins Science Protein subunit General Physics and Astronomy 02 engineering and technology Wobble base pair Article General Biochemistry Genetics and Molecular Biology ELP3 Substrate Specificity 03 medical and health sciences RNA Transfer Catalytic Domain Transferase lcsh:Science Histone Acetyltransferases Multidisciplinary biology Chemistry Active site General Chemistry 021001 nanoscience & nanotechnology 030104 developmental biology Biochemistry Acetyltransferase Methanocaldococcus Transfer RNA biology.protein lcsh:Q ddc:500 0210 nano-technology |
| Zdroj: | Nature Communications 10(1), 625 (2019). doi:10.1038/s41467-019-08579-2 Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019) Nature Communications |
| DOI: | 10.3204/pubdb-2019-01203 |
| Popis: | Nature Communications 10(1), 625 (2019). doi:10.1038/s41467-019-08579-2 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. Published by Nature Publishing , London |
| Databáze: | OpenAIRE |
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