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000602296 1001_ $$0P:(DE-HGF)0$$aJaciuk, Marcin$$b0
000602296 245__ $$aCryo-EM structure of the fully assembled Elongator complex
000602296 260__ $$aOxford$$bOxford Univ. Press$$c2023
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000602296 520__ $$aTransfer RNA (tRNA) molecules are essential to decode messenger RNA codons during protein synthesis. All known tRNAs are heavily modified at multiple positions through post-transcriptional addition of chemical groups. Modifications in the tRNA anticodons are directly influencing ribosome decoding and dynamics during translation elongation and are crucial for maintaining proteome integrity. In eukaryotes, wobble uridines are modified by Elongator, a large and highly conserved macromolecular complex. Elongator consists of two subcomplexes, namely Elp123 containing the enzymatically active Elp3 subunit and the associated Elp456 hetero-hexamer. The structure of the fully assembled complex and the function of the Elp456 subcomplex have remained elusive. Here, we show the cryo-electron microscopy structure of yeast Elongator at an overall resolution of 4.3 Å. We validate the obtained structure by complementary mutational analyses in vitro and in vivo. In addition, we determined various structures of the murine Elongator complex, including the fully assembled mouse Elongator complex at 5.9 Å resolution. Our results confirm the structural conservation of Elongator and its intermediates among eukaryotes. Furthermore, we complement our analyses with the biochemical characterization of the assembled human Elongator. Our results provide the molecular basis for the assembly of Elongator and its tRNA modification activity in eukaryotes. 
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000602296 7001_ $$0P:(DE-HGF)0$$aScherf, David$$b1
000602296 7001_ $$0P:(DE-HGF)0$$aKaszuba, Karol$$b2
000602296 7001_ $$0P:(DE-HGF)0$$aGaik, Monika$$b3
000602296 7001_ $$0P:(DE-H253)PIP1021275$$aRau, Alexander$$b4
000602296 7001_ $$0P:(DE-HGF)0$$aKościelniak, Anna$$b5
000602296 7001_ $$0P:(DE-HGF)0$$aKrutyhołowa, Rościsław$$b6
000602296 7001_ $$0P:(DE-HGF)0$$aRawski, Michał$$b7
000602296 7001_ $$0P:(DE-HGF)0$$aIndyka, Paulina$$b8
000602296 7001_ $$0P:(DE-H253)PIP1080677$$aGraziadei, Andrea$$b9
000602296 7001_ $$0P:(DE-HGF)0$$aChramiec-Głąbik, Andrzej$$b10
000602296 7001_ $$0P:(DE-HGF)0$$aBiela, Anna$$b11
000602296 7001_ $$0P:(DE-HGF)0$$aDobosz, Dominika$$b12
000602296 7001_ $$0P:(DE-HGF)0$$aLin, Ting-Yu$$b13
000602296 7001_ $$0P:(DE-H253)PIP1084330$$aAbbassi, Nour-el-Hana$$b14
000602296 7001_ $$0P:(DE-HGF)0$$aHammermeister, Alexander$$b15
000602296 7001_ $$0P:(DE-HGF)0$$aRappsilber, Juri$$b16
000602296 7001_ $$0P:(DE-H253)PIP1081584$$aKosinski, Jan$$b17
000602296 7001_ $$0P:(DE-HGF)0$$aSchaffrath, Raffael$$b18
000602296 7001_ $$0P:(DE-HGF)0$$aGlatt, Sebastian$$b19$$eCorresponding author
000602296 773__ $$0PERI:(DE-600)2205588-5$$a10.1093/nar/gkac1232$$gVol. 51, no. 5, p. 2011 - 2032$$n5$$p2011 - 2032$$tNucleic acids symposium series$$v51$$x0305-1048$$y2023
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