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Yorodumi- EMDB-12908: Nog1-TAP associated immature ribosomal particles from S. cerevisi... -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-12908 | |||||||||
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| Title | Nog1-TAP associated immature ribosomal particles from S. cerevisiae after rpL2 expression shut down, population A | |||||||||
Map data | Nog1-TAP associated immature ribosomal particles from S. cerevisiae after rpL2 expression shut down, population A, full map | |||||||||
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Keywords | ribosomal assembly state / RIBOSOME | |||||||||
| Function / homology | Function and homology informationprotein-RNA complex remodeling / regulation of ribosomal subunit export from nucleus / 7S RNA binding / positive regulation of ATP-dependent activity / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of 5.8S rRNA / ribosomal large subunit binding / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) ...protein-RNA complex remodeling / regulation of ribosomal subunit export from nucleus / 7S RNA binding / positive regulation of ATP-dependent activity / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of 5.8S rRNA / ribosomal large subunit binding / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / preribosome, large subunit precursor / ATPase activator activity / Formation of a pool of free 40S subunits / nuclear-transcribed mRNA catabolic process / L13a-mediated translational silencing of Ceruloplasmin expression / translational elongation / ribosomal large subunit export from nucleus / ribosomal subunit export from nucleus / maturation of LSU-rRNA / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / translation initiation factor activity / nuclear periphery / assembly of large subunit precursor of preribosome / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / cytosolic ribosome assembly / maturation of SSU-rRNA / macroautophagy / small-subunit processome / maintenance of translational fidelity / rRNA processing / ATPase binding / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / GTPase activity / mRNA binding / GTP binding / nucleolus / RNA binding / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() ![]() ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.7 Å | |||||||||
Authors | Milkereit P / Poell G | |||||||||
| Funding support | Germany, 1 items
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Citation | Journal: PLoS One / Year: 2021Title: Analysis of subunit folding contribution of three yeast large ribosomal subunit proteins required for stabilisation and processing of intermediate nuclear rRNA precursors. Authors: Gisela Pöll / Michael Pilsl / Joachim Griesenbeck / Herbert Tschochner / Philipp Milkereit / ![]() Abstract: In yeast and human cells many of the ribosomal proteins (r-proteins) are required for the stabilisation and productive processing of rRNA precursors. Functional coupling of r-protein assembly with ...In yeast and human cells many of the ribosomal proteins (r-proteins) are required for the stabilisation and productive processing of rRNA precursors. Functional coupling of r-protein assembly with the stabilisation and maturation of subunit precursors potentially promotes the production of ribosomes with defined composition. To further decipher mechanisms of such an intrinsic quality control pathway we analysed here the contribution of three yeast large ribosomal subunit r-proteins rpL2 (uL2), rpL25 (uL23) and rpL34 (eL34) for intermediate nuclear subunit folding steps. Structure models obtained from single particle cryo-electron microscopy analyses provided evidence for specific and hierarchic effects on the stable positioning and remodelling of large ribosomal subunit domains. Based on these structural and previous biochemical data we discuss possible mechanisms of r-protein dependent hierarchic domain arrangement and the resulting impact on the stability of misassembled subunits. | |||||||||
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_12908.map.gz | 192.7 MB | EMDB map data format | |
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| Header (meta data) | emd-12908-v30.xml emd-12908.xml | 51 KB 51 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_12908_fsc.xml | 14.3 KB | Display | FSC data file |
| Images | emd_12908.png | 104.3 KB | ||
| Filedesc metadata | emd-12908.cif.gz | 12.5 KB | ||
| Others | emd_12908_half_map_1.map.gz emd_12908_half_map_2.map.gz | 194.6 MB 194.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-12908 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-12908 | HTTPS FTP |
-Validation report
| Summary document | emd_12908_validation.pdf.gz | 1008.8 KB | Display | EMDB validaton report |
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| Full document | emd_12908_full_validation.pdf.gz | 1008.4 KB | Display | |
| Data in XML | emd_12908_validation.xml.gz | 21.8 KB | Display | |
| Data in CIF | emd_12908_validation.cif.gz | 28.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-12908 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-12908 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7ohtMC ![]() 7of1C ![]() 7oh3C ![]() 7ohpC ![]() 7ohqC ![]() 7ohrC ![]() 7ohsC ![]() 7ohuC ![]() 7ohvC ![]() 7ohwC ![]() 7ohxC ![]() 7ohyC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | |
| EM raw data | EMPIAR-10780 (Title: Nog1-TAP associated immature ribosomal particles from S.cerevisae depleted of rpL2Data size: 4.9 TB Data #1: Unaligned multiframe micrographs of Nog1-TAP associated immature ribosomal particles from S. cerevisisae depleted of rpL2 [micrographs - multiframe]) |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_12908.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | Nog1-TAP associated immature ribosomal particles from S. cerevisiae after rpL2 expression shut down, population A, full map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.0635 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: Nog1-TAP associated immature ribosomal particles from S. cerevisiae...
| File | emd_12908_half_map_1.map | ||||||||||||
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| Annotation | Nog1-TAP associated immature ribosomal particles from S. cerevisiae after rpL2 expression shut down, population A, half map 1 | ||||||||||||
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| Density Histograms |
-Half map: Nog1-TAP associated immature ribosomal particles from S. cerevisiae...
| File | emd_12908_half_map_2.map | ||||||||||||
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| Annotation | Nog1-TAP associated immature ribosomal particles from S. cerevisiae after rpL2 expression shut down, population A, half map 2 | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : Nog1-TAP associated immature ribosomal particles from cells deple...
+Supramolecule #1: Nog1-TAP associated immature ribosomal particles from cells deple...
+Macromolecule #1: 25S rRNA
+Macromolecule #2: 5.8S rRNA
+Macromolecule #3: 5S rRNA
+Macromolecule #4: 60S ribosomal protein L3
+Macromolecule #5: 60S ribosomal protein L4-A
+Macromolecule #6: 60S ribosomal protein L5
+Macromolecule #7: 60S ribosomal protein L6-A
+Macromolecule #8: 60S ribosomal protein L7-A
+Macromolecule #9: 60S ribosomal protein L9-A
+Macromolecule #10: 60S ribosomal protein L11-A
+Macromolecule #11: 60S ribosomal protein L14-A
+Macromolecule #12: 60S ribosomal protein L16-A
+Macromolecule #13: 60S ribosomal protein L18-A
+Macromolecule #14: 60S ribosomal protein L20-A
+Macromolecule #15: 60S ribosomal protein L21-A
+Macromolecule #16: 60S ribosomal protein L23-A
+Macromolecule #17: Ribosome assembly factor MRT4
+Macromolecule #18: Nucleolar GTP-binding protein 1
+Macromolecule #19: 60S ribosomal protein L32
+Macromolecule #20: 60S ribosomal protein L33-A
+Macromolecule #21: Nucleolar GTP-binding protein 2
+Macromolecule #22: Ribosome biogenesis protein NSA2
+Macromolecule #23: Ribosome biogenesis protein RLP24
+Macromolecule #24: Ribosome biogenesis protein RPF2
+Macromolecule #25: Regulator of ribosome biosynthesis
+Macromolecule #26: Ribosome assembly protein 4
+Macromolecule #27: Eukaryotic translation initiation factor 6
+Macromolecule #28: MAGNESIUM ION
+Macromolecule #29: ZINC ION
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 Component:
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| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 200 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.4 kPa | ||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Average exposure time: 5.16 sec. / Average electron dose: 86.45 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Keywords
Authors
Germany, 1 items
Citation
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