8jdm

Structure of the Human cytoplasmic Ribosome with human tRNA Tyr(GalQ34) and mRNA(UAU) (rotated state)

spinqualitylabelsall models 8jdm, resolution 2.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8jdm is a 11 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.67Å Ligands: 1MA, 1MG, 2MG, 3AU, 4AC, 56B, 5MC, 5MU, 6MZ, A2M, B8N, G7M, GAL, H2U, M2G, MA6, MG, OMC, OMG, OMU, PSU, UR3, UY1, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL8_HUMAN Publication Abstract from PubMed Transfer RNA (tRNA) modifications are critical for protein synthesis. Queuosine (Q), a 7-deaza-guanosine derivative, is present in tRNA anticodons. In vertebrate tRNAs for Tyr and Asp, Q is further glycosylated with galactose and mannose to generate galQ and manQ, respectively. However, biogenesis and physiological relevance of Q-glycosylation remain poorly understood. Here, we biochemically identified two RNA glycosylases, QTGAL and QTMAN, and successfully reconstituted Q-glycosylation of tRNAs using nucleotide diphosphate sugars. Ribosome profiling of knockout cells revealed that Q-glycosylation slowed down elongation at cognate codons, UAC and GAC (GAU), respectively. We also found that galactosylation of Q suppresses stop codon readthrough. Moreover, protein aggregates increased in cells lacking Q-glycosylation, indicating that Q-glycosylation contributes to proteostasis. Cryo-EM of human ribosome-tRNA complex revealed the molecular basis of codon recognition regulated by Q-glycosylations. Furthermore, zebrafish qtgal and qtman knockout lines displayed shortened body length, implying that Q-glycosylation is required for post-embryonic growth in vertebrates. Glycosylated queuosines in tRNAs optimize translational rate and post-embryonic growth.,Zhao X, Ma D, Ishiguro K, Saito H, Akichika S, Matsuzawa I, Mito M, Irie T, Ishibashi K, Wakabayashi K, Sakaguchi Y, Yokoyama T, Mishima Y, Shirouzu M, Iwasaki S, Suzuki T, Suzuki T Cell. 2023 Dec 7;186(25):5517-5535.e24. doi: 10.1016/j.cell.2023.10.026. Epub , 2023 Nov 21. PMID:37992713 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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