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-Structure paper
タイトル | CryoEM structures of pseudouridine-free ribosome suggest impacts of chemical modifications on ribosome conformations. |
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ジャーナル・号・ページ | Structure, Vol. 30, Issue 7, Page 983-992.e5, Year 2022 |
掲載日 | 2022年7月7日 |
著者 | Yu Zhao / Jay Rai / Hongguo Yu / Hong Li / |
PubMed 要旨 | Pseudouridine, the most abundant form of RNA modification, is known to play important roles in ribosome function. Mutations in human DKC1, the pseudouridine synthase responsible for catalyzing the ...Pseudouridine, the most abundant form of RNA modification, is known to play important roles in ribosome function. Mutations in human DKC1, the pseudouridine synthase responsible for catalyzing the ribosome RNA modification, cause translation deficiencies and are associated with a complex cancer predisposition. The structural basis for how pseudouridine impacts ribosome function remains uncharacterized. Here, we characterized structures and conformations of a fully modified and a pseudouridine-free ribosome from Saccharomyces cerevisiae in the absence of ligands or when bound with translocation inhibitor cycloheximide by electron cryomicroscopy. In the modified ribosome, the rearranged N1 atom of pseudouridine is observed to stabilize key functional motifs by establishing predominately water-mediated close contacts with the phosphate backbone. The pseudouridine-free ribosome, however, is devoid of such interactions and displays conformations reflective of abnormal inter-subunit movements. The erroneous motions of the pseudouridine-free ribosome may explain its observed deficiencies in translation. |
リンク | Structure / PubMed:35489333 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.7 - 3.05 Å |
構造データ | EMDB-23934, PDB-7mpi: EMDB-23935, PDB-7mpj: EMDB-24235, PDB-7n8b: |
化合物 | ChemComp-MG: ChemComp-ZN: ChemComp-3HE: |
由来 |
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キーワード | RIBOSOME / yeast / 80S complex / chemical modification |