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Open data
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Basic information
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Title | Yeast RQC complex in state D | |||||||||
![]() | Yeast RQC complex in state D, half map B | |||||||||
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![]() | ribosome-associated quality control / NEMF / Listerin / CAT tailing / TRANSLATION | |||||||||
Function / homology | ![]() RQC complex / ribosome-associated ubiquitin-dependent protein catabolic process / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / pre-mRNA 5'-splice site binding / cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / response to cycloheximide / maturation of 5.8S rRNA / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / ribosomal large subunit binding ...RQC complex / ribosome-associated ubiquitin-dependent protein catabolic process / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / pre-mRNA 5'-splice site binding / cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / response to cycloheximide / maturation of 5.8S rRNA / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / ribosomal large subunit binding / Formation of a pool of free 40S subunits / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / negative regulation of mRNA splicing, via spliceosome / Antigen processing: Ubiquitination & Proteasome degradation / L13a-mediated translational silencing of Ceruloplasmin expression / preribosome, large subunit precursor / translational elongation / ribosomal large subunit export from nucleus / subtelomeric heterochromatin formation / 90S preribosome / protein-RNA complex assembly / regulation of translational fidelity / proteasomal protein catabolic process / ribosomal subunit export from nucleus / cytosolic ribosome / translation initiation factor activity / maturation of LSU-rRNA / rescue of stalled ribosome / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / assembly of large subunit precursor of preribosome / cytosolic ribosome assembly / ribosomal large subunit biogenesis / translational initiation / macroautophagy / maintenance of translational fidelity / RING-type E3 ubiquitin transferase / protein catabolic process / modification-dependent protein catabolic process / rRNA processing / protein tag activity / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / ribosome biogenesis / chromatin organization / chromosome, telomeric region / 5S rRNA binding / large ribosomal subunit rRNA binding / ubiquitin-dependent protein catabolic process / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / rRNA binding / negative regulation of translation / ribosome / protein ubiquitination / structural constituent of ribosome / translation / response to antibiotic / mRNA binding / ubiquitin protein ligase binding / nucleolus / RNA binding / zinc ion binding / nucleus / metal ion binding / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.6 Å | |||||||||
![]() | Tesina P / Buschauer R / Beckmann R | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular basis of eIF5A-dependent CAT tailing in eukaryotic ribosome-associated quality control. Authors: Petr Tesina / Shuhei Ebine / Robert Buschauer / Matthias Thoms / Yoshitaka Matsuo / Toshifumi Inada / Roland Beckmann / ![]() ![]() Abstract: Ribosome-associated quality control (RQC) is a conserved process degrading potentially toxic truncated nascent peptides whose malfunction underlies neurodegeneration and proteostasis decline in aging. ...Ribosome-associated quality control (RQC) is a conserved process degrading potentially toxic truncated nascent peptides whose malfunction underlies neurodegeneration and proteostasis decline in aging. During RQC, dissociation of stalled ribosomes is followed by elongation of the nascent peptide with alanine and threonine residues, driven by Rqc2 independently of mRNA, the small ribosomal subunit and guanosine triphosphate (GTP)-hydrolyzing factors. The resulting CAT tails (carboxy-terminal tails) and ubiquitination by Ltn1 mark nascent peptides for proteasomal degradation. Here we present ten cryogenic electron microscopy (cryo-EM) structures, revealing the mechanistic basis of individual steps of the CAT tailing cycle covering initiation, decoding, peptidyl transfer, and tRNA translocation. We discovered eIF5A as a crucial eukaryotic RQC factor enabling peptidyl transfer. Moreover, we observed dynamic behavior of RQC factors and tRNAs allowing for processivity of the CAT tailing cycle without additional energy input. Together, these results elucidate key differences as well as common principles between CAT tailing and canonical translation. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 20.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 72.9 KB 72.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 15.6 KB | Display | ![]() |
Images | ![]() | 62.3 KB | ||
Filedesc metadata | ![]() | 15.4 KB | ||
Others | ![]() ![]() | 322.6 MB 322.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8agwMC ![]() 8aafC ![]() 8agtC ![]() 8aguC ![]() 8agvC ![]() 8agxC ![]() 8agzC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | Yeast RQC complex in state D, half map B | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.059 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Yeast RQC complex in state D, half map A
File | emd_15426_half_map_1.map | ||||||||||||
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Annotation | Yeast RQC complex in state D, half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Yeast RQC complex in state D
File | emd_15426_half_map_2.map | ||||||||||||
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Annotation | Yeast RQC complex in state D | ||||||||||||
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Density Histograms |
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Sample components
+Entire : Yeast RQC complex in state D
+Supramolecule #1: Yeast RQC complex in state D
+Macromolecule #1: 60S ribosomal protein L15-A
+Macromolecule #2: 60S ribosomal protein L16-A
+Macromolecule #3: 60S ribosomal protein L17-A
+Macromolecule #4: 60S ribosomal protein L18-A
+Macromolecule #5: 60S ribosomal protein L19-A
+Macromolecule #6: 60S ribosomal protein L20-A
+Macromolecule #7: 60S ribosomal protein L21-A
+Macromolecule #8: 60S ribosomal protein L22-A
+Macromolecule #9: 60S ribosomal protein L23-A
+Macromolecule #10: 60S ribosomal protein L24-A
+Macromolecule #11: 60S ribosomal protein L25
+Macromolecule #12: 60S ribosomal protein L26-A
+Macromolecule #13: 60S ribosomal protein L27-A
+Macromolecule #14: 60S ribosomal protein L28
+Macromolecule #15: 60S ribosomal protein L29
+Macromolecule #16: 60S ribosomal protein L30
+Macromolecule #17: 60S ribosomal protein L31-A
+Macromolecule #18: 60S ribosomal protein L32
+Macromolecule #19: 60S ribosomal protein L33-A
+Macromolecule #20: 60S ribosomal protein L34-A
+Macromolecule #21: 60S ribosomal protein L35-A
+Macromolecule #22: 60S ribosomal protein L36-A
+Macromolecule #23: 60S ribosomal protein L37-A
+Macromolecule #24: 60S ribosomal protein L38
+Macromolecule #25: 60S ribosomal protein L39
+Macromolecule #26: Ubiquitin-60S ribosomal protein L40
+Macromolecule #27: 60S ribosomal protein L42-A
+Macromolecule #28: 60S ribosomal protein L43-A
+Macromolecule #29: 60S ribosomal protein L41-A
+Macromolecule #33: 60S ribosomal protein L2-A
+Macromolecule #34: 60S ribosomal protein L3
+Macromolecule #35: 60S ribosomal protein L4-A
+Macromolecule #36: 60S ribosomal protein L5
+Macromolecule #37: 60S ribosomal protein L6-B
+Macromolecule #38: 60S ribosomal protein L7-A
+Macromolecule #39: 60S ribosomal protein L8-A
+Macromolecule #40: 60S ribosomal protein L9-A
+Macromolecule #41: 60S ribosomal protein L10
+Macromolecule #42: 60S ribosomal protein L11-A
+Macromolecule #43: 60S ribosomal protein L13-A
+Macromolecule #44: 60S ribosomal protein L14-A
+Macromolecule #45: RQC2 isoform 1
+Macromolecule #46: E3 ubiquitin-protein ligase listerin
+Macromolecule #47: Eukaryotic translation initiation factor 6
+Macromolecule #49: 60S ribosomal protein L12-A
+Macromolecule #50: 60S acidic ribosomal protein P0
+Macromolecule #51: CAT-tailed nascent peptide
+Macromolecule #52: 60S ribosomal protein L1-A
+Macromolecule #30: 25S rRNA
+Macromolecule #31: 5S rRNA
+Macromolecule #32: 5.8S rRNA
+Macromolecule #48: Ala tRNA
+Macromolecule #53: MAGNESIUM ION
+Macromolecule #54: ZINC ION
+Macromolecule #55: SPERMIDINE
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 6.8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 46.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 0.4 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |