The deposited data concern the mapping of acetylation sites on wild-type and the K280A, Y363A mutants of Elp3 by LC-MS/MS.
Abstract of the manuscript:
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 cycle. The structures at resolutions of up to 2.9 A 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 (ACO) 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 first high-resolution view of human Elongator and reveal its detailed mechanism of action.
[doi:10.25345/C5N01044H]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Elp3 ; Elongator complex ; Acetylation
Principal Investigators: (in alphabetical order) |
Sebastian Glatt, Malopolska Centre of Biotechnology (MCB), Jagiellonian University, Poland |
Submitting User: | Urszula |
Abbassi NE, Jaciuk M, Scherf D, Böhnert P, Rau A, Hammermeister A, Rawski M, Indyka P, Wazny G, Chramiec-G??bik A, Dobosz D, Skupien-Rabian B, Jankowska U, Rappsilber J, Schaffrath R, Lin TY, Glatt S.
Cryo-EM structures of the human Elongator complex at work.
Nat Commun. 2024 May 15;15(1):4094. Epub 2024 May 15.
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