TY  - JOUR
AU  - Jaciuk, Marcin
AU  - Scherf, David
AU  - Kaszuba, Karol
AU  - Gaik, Monika
AU  - Rau, Alexander
AU  - Kościelniak, Anna
AU  - Krutyhołowa, Rościsław
AU  - Rawski, Michał
AU  - Indyka, Paulina
AU  - Graziadei, Andrea
AU  - Chramiec-Głąbik, Andrzej
AU  - Biela, Anna
AU  - Dobosz, Dominika
AU  - Lin, Ting-Yu
AU  - Abbassi, Nour-el-Hana
AU  - Hammermeister, Alexander
AU  - Rappsilber, Juri
AU  - Kosinski, Jan
AU  - Schaffrath, Raffael
AU  - Glatt, Sebastian
TI  - Cryo-EM structure of the fully assembled Elongator complex
JO  - Nucleic acids symposium series
VL  - 51
IS  - 5
SN  - 0305-1048
CY  - Oxford
PB  - Oxford Univ. Press
M1  - PUBDB-2024-00571
SP  - 2011 - 2032
PY  - 2023
N1  - ISSN 1362-4962 not unique: **2 hits**.
AB  - Transfer 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. 
LB  - PUB:(DE-HGF)16
C6  - pmid:36617428
UR  - <Go to ISI:>//WOS:000912446800001
DO  - DOI:10.1093/nar/gkac1232
UR  - https://bib-pubdb1.desy.de/record/602296
ER  -