Cryo-EM structures of the human Elongator complex at work

Nour-el-Hana Abbassi, Marcin Jaciuk, David Scherf, Pauline Böhnert, Alexander Rau, Alexander Hammermeister, Michał Rawski, Paulina Indyka, Grzegorz Wazny, Andrzej Chramiec-Głąbik, Dominika Dobosz, Bozena Skupien-Rabian, Urszula Jankowska, Juri Rappsilber, Raffael Schaffrath (), Ting-Yu Lin () and Sebastian Glatt ()
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Nour-el-Hana Abbassi: Jagiellonian University
Marcin Jaciuk: Jagiellonian University
David Scherf: University of Kassel
Pauline Böhnert: University of Kassel
Alexander Rau: Technical University of Berlin
Alexander Hammermeister: Jagiellonian University
Michał Rawski: Jagiellonian University
Paulina Indyka: Jagiellonian University
Grzegorz Wazny: Jagiellonian University
Andrzej Chramiec-Głąbik: Jagiellonian University
Dominika Dobosz: Jagiellonian University
Bozena Skupien-Rabian: Jagiellonian University
Urszula Jankowska: Jagiellonian University
Juri Rappsilber: Technical University of Berlin
Raffael Schaffrath: University of Kassel
Ting-Yu Lin: Jagiellonian University
Sebastian Glatt: Jagiellonian University

Nature Communications, 2024, vol. 15, issue 1, 1-16

Abstract: Abstract tRNA modifications affect ribosomal elongation speed and co-translational folding dynamics. The Elongator complex is responsible for introducing 5-carboxymethyl at wobble uridine bases (cm5U34) in eukaryotic tRNAs. However, the structure and function of human Elongator remain poorly understood. In this study, we present a series of cryo-EM structures of human ELP123 in complex with tRNA and cofactors at four different stages of the reaction. The structures at resolutions of up to 2.9 Å together with complementary functional analyses reveal the molecular mechanism of the modification reaction. Our results show that tRNA binding exposes a universally conserved uridine at position 33 (U33), which triggers acetyl-CoA hydrolysis. We identify a series of conserved residues that are crucial for the radical-based acetylation of U34 and profile the molecular effects of patient-derived mutations. Together, we provide the high-resolution view of human Elongator and reveal its detailed mechanism of action.

Date: 2024
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DOI: 10.1038/s41467-024-48251-y

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