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Yorodumi- EMDB-13954: Neuronal RNA granules are ribosome complexes stalled at the pre-t... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-13954 | ||||||||||||
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Title | Neuronal RNA granules are ribosome complexes stalled at the pre-translocation state | ||||||||||||
Map data | Postprocessed map (Relion) of rat ribosome from neuronal RNA granules. | ||||||||||||
Sample |
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Keywords | Ribosome / RNA granule / rat | ||||||||||||
Function / homology | Function and homology information regulation of myeloid dendritic cell activation / positive regulation of selenocysteine incorporation / Protein hydroxylation / mTORC1-mediated signalling / Translesion synthesis by REV1 / Recognition of DNA damage by PCNA-containing replication complex / APC/C:Cdc20 mediated degradation of Cyclin B / APC-Cdc20 mediated degradation of Nek2A / Activated NOTCH1 Transmits Signal to the Nucleus / Downregulation of TGF-beta receptor signaling ...regulation of myeloid dendritic cell activation / positive regulation of selenocysteine incorporation / Protein hydroxylation / mTORC1-mediated signalling / Translesion synthesis by REV1 / Recognition of DNA damage by PCNA-containing replication complex / APC/C:Cdc20 mediated degradation of Cyclin B / APC-Cdc20 mediated degradation of Nek2A / Activated NOTCH1 Transmits Signal to the Nucleus / Downregulation of TGF-beta receptor signaling / Regulation of FZD by ubiquitination / Regulation of TNFR1 signaling / TNFR1-induced NF-kappa-B signaling pathway / Translesion synthesis by POLK / Translesion synthesis by POLI / Termination of translesion DNA synthesis / Gap-filling DNA repair synthesis and ligation in GG-NER / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / Fanconi Anemia Pathway / Regulation of TP53 Degradation / Regulation of TP53 Activity through Methylation / Cyclin D associated events in G1 / Stabilization of p53 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / ER Quality Control Compartment (ERQC) / Interferon alpha/beta signaling / Endosomal Sorting Complex Required For Transport (ESCRT) / Negative regulators of DDX58/IFIH1 signaling / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / IKK complex recruitment mediated by RIP1 / IRAK2 mediated activation of TAK1 complex / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Alpha-protein kinase 1 signaling pathway / Inactivation of CSF3 (G-CSF) signaling / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Regulation of NF-kappa B signaling / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / NOD1/2 Signaling Pathway / activated TAK1 mediates p38 MAPK activation / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / DNA Damage Recognition in GG-NER / Formation of Incision Complex in GG-NER / Dual Incision in GG-NER / E3 ubiquitin ligases ubiquitinate target proteins / Translesion Synthesis by POLH / Downregulation of ERBB2:ERBB3 signaling / TCF dependent signaling in response to WNT / Regulation of innate immune responses to cytosolic DNA / HDR through Homologous Recombination (HRR) / Downregulation of ERBB2 signaling / Regulation of signaling by CBL / Ovarian tumor domain proteases / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / NOTCH3 Activation and Transmission of Signal to the Nucleus / Interleukin-1 signaling / cellular response to Thyroid stimulating hormone / Downregulation of ERBB4 signaling / Deactivation of the beta-catenin transactivating complex / Negative regulation of MET activity / Translation initiation complex formation / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / Protein methylation / Regulation of PTEN localization / L13a-mediated translational silencing of Ceruloplasmin expression / SRP-dependent cotranslational protein targeting to membrane / Josephin domain DUBs / Formation of a pool of free 40S subunits / 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) / RMTs methylate histone arginines / Major pathway of rRNA processing in the nucleolus and cytosol / Pexophagy / Stimuli-sensing channels / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / 5.8S rRNA binding / Metalloprotease DUBs / Regulation of necroptotic cell death / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Autodegradation of Cdh1 by Cdh1:APC/C / SCF-beta-TrCP mediated degradation of Emi1 / APC/C:Cdc20 mediated degradation of Securin / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / SCF(Skp2)-mediated degradation of p27/p21 / NRIF signals cell death from the nucleus / NF-kB is activated and signals survival / Autodegradation of the E3 ubiquitin ligase COP1 / Asymmetric localization of PCP proteins / Degradation of DVL / Hedgehog ligand biogenesis / Dectin-1 mediated noncanonical NF-kB signaling / Degradation of GLI1 by the proteasome / Hedgehog 'on' state / TNFR2 non-canonical NF-kB pathway / NIK-->noncanonical NF-kB signaling Similarity search - Function | ||||||||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.86 Å | ||||||||||||
Authors | Pulk A / Kipper K / Mansour A | ||||||||||||
Funding support | Estonia, 3 items
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Citation | Journal: J Mol Biol / Year: 2022 Title: Neuronal RNA granules are ribosome complexes stalled at the pre-translocation state. Authors: Kalle Kipper / Abbas Mansour / Arto Pulk / Abstract: The polarized cell morphology of neurons dictates many neuronal processes, including the axodendridic transport of specific mRNAs and subsequent translation. mRNAs together with ribosomes and RNA- ...The polarized cell morphology of neurons dictates many neuronal processes, including the axodendridic transport of specific mRNAs and subsequent translation. mRNAs together with ribosomes and RNA-binding proteins form RNA granules that are targeted to axodendrites for localized translation in neurons. It has been established that localized protein synthesis in neurons is essential for long-term memory formation, synaptic plasticity, and neurodegeneration. We have used proteomics and electron microscopy to characterize neuronal RNA granules (nRNAg) isolated from rat brain tissues or human neuroblastoma. We show that ribosome-containing RNA granules are morula-like structures when visualized by electron microscopy. Crosslinking-coupled mass-spectrometry identified a potential G3BP2 binding site on the ribosome near the eIF3d-binding site on the 40S ribosomal subunit. We used cryo-EM to resolve the structure of the ribosome-component of nRNAg. The cryo-EM reveals that predominant particles in nRNAg are 80S ribosomes, resembling the pre-translocation state where tRNA's are in the hybrid A/P and P/E site. We also describe a new kind of principal motion of the ribosome, which we call the rocking motion. | ||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_13954.map.gz | 17.5 MB | EMDB map data format | |
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Header (meta data) | emd-13954-v30.xml emd-13954.xml | 106.6 KB 106.6 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_13954_fsc.xml | 10.5 KB | Display | FSC data file |
Images | emd_13954.png | 65 KB | ||
Masks | emd_13954_msk_1.map | 101 MB | Mask map | |
Filedesc metadata | emd-13954.cif.gz | 21.5 KB | ||
Others | emd_13954_additional_1.map.gz | 63.2 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-13954 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-13954 | HTTPS FTP |
-Validation report
Summary document | emd_13954_validation.pdf.gz | 553 KB | Display | EMDB validaton report |
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Full document | emd_13954_full_validation.pdf.gz | 552.6 KB | Display | |
Data in XML | emd_13954_validation.xml.gz | 11.8 KB | Display | |
Data in CIF | emd_13954_validation.cif.gz | 15.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13954 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13954 | HTTPS FTP |
-Related structure data
Related structure data | 7qggMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_13954.map.gz / Format: CCP4 / Size: 101 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Postprocessed map (Relion) of rat ribosome from neuronal RNA granules. | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.41 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_13954_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: Sharpened map (Phenix) used to RealSpace refine the coordinates.
File | emd_13954_additional_1.map | ||||||||||||
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Annotation | Sharpened map (Phenix) used to RealSpace refine the coordinates. | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Ribosome structure in the rat cortex-hippocampus derived neuronal...
+Supramolecule #1: Ribosome structure in the rat cortex-hippocampus derived neuronal...
+Macromolecule #1: RNA (1872-MER)
+Macromolecule #38: RNA (157-MER)
+Macromolecule #39: RNA (121-MER)
+Macromolecule #79: RNA (4803-MER)
+Macromolecule #80: RNA (76-MER)
+Macromolecule #81: RNA (76-MER)
+Macromolecule #82: RNA (5'-D(P*()P*()P*()P*())-R(P*UP*UP*AP*CP*GP*GP*CP*GP*GP*UP*()P...
+Macromolecule #2: 40S ribosomal protein SA
+Macromolecule #3: 40S ribosomal protein S3a
+Macromolecule #4: 40S ribosomal protein S3
+Macromolecule #5: 40S ribosomal protein S4, X isoform
+Macromolecule #6: 40S ribosomal protein S5
+Macromolecule #7: 40S ribosomal protein S7
+Macromolecule #8: 40S ribosomal protein S8
+Macromolecule #9: 40S ribosomal protein S10
+Macromolecule #10: 40S ribosomal protein S11
+Macromolecule #11: 40S ribosomal protein S15
+Macromolecule #12: Rps16 protein
+Macromolecule #13: 40S ribosomal protein S17
+Macromolecule #14: 40S ribosomal protein S18
+Macromolecule #15: 40S ribosomal protein S19
+Macromolecule #16: 40S ribosomal protein S20
+Macromolecule #17: 40S ribosomal protein S21
+Macromolecule #18: 40S ribosomal protein S23
+Macromolecule #19: 40S ribosomal protein S26
+Macromolecule #20: 40S ribosomal protein S28
+Macromolecule #21: 40S ribosomal protein S29
+Macromolecule #22: Receptor of activated protein C kinase 1
+Macromolecule #23: 40S ribosomal protein S2
+Macromolecule #24: 40S ribosomal protein S6
+Macromolecule #25: 40S ribosomal protein S9
+Macromolecule #26: 40S ribosomal protein S12
+Macromolecule #27: 40S ribosomal protein S13
+Macromolecule #28: 40S ribosomal protein S14
+Macromolecule #29: 40S ribosomal protein S15a
+Macromolecule #30: 40S ribosomal protein S24
+Macromolecule #31: 40S ribosomal protein S25
+Macromolecule #32: 40S ribosomal protein S27
+Macromolecule #33: Ubiquitin-like domain-containing protein
+Macromolecule #34: Ubiquitin-40S ribosomal protein S27a
+Macromolecule #35: 60S ribosomal protein L8
+Macromolecule #36: 60S ribosomal protein L3
+Macromolecule #37: 60S ribosomal protein L4
+Macromolecule #40: 60S ribosomal protein L5
+Macromolecule #41: 60S ribosomal protein L6
+Macromolecule #42: 60S ribosomal protein L7
+Macromolecule #43: 60S ribosomal protein L7a
+Macromolecule #44: 60S ribosomal protein L9
+Macromolecule #45: 60S ribosomal protein L10
+Macromolecule #46: 60S ribosomal protein L11
+Macromolecule #47: 60S ribosomal protein L13
+Macromolecule #48: 60S ribosomal protein L14
+Macromolecule #49: Ribosomal protein L15
+Macromolecule #50: 60S ribosomal protein L13a
+Macromolecule #51: 60S ribosomal protein L17
+Macromolecule #52: 60S ribosomal protein L18
+Macromolecule #53: Ribosomal protein L19
+Macromolecule #54: 60S ribosomal protein L18a
+Macromolecule #55: 60S ribosomal protein L21
+Macromolecule #56: 60S ribosomal protein L22
+Macromolecule #57: 60S ribosomal protein L23
+Macromolecule #58: 60S ribosomal protein L24
+Macromolecule #59: 60S ribosomal protein L23a
+Macromolecule #60: 60S ribosomal protein L26
+Macromolecule #61: 60S ribosomal protein L27
+Macromolecule #62: 60S ribosomal protein L27a
+Macromolecule #63: 60S ribosomal protein L29
+Macromolecule #64: 60S ribosomal protein L30
+Macromolecule #65: 60S ribosomal protein L31
+Macromolecule #66: 60S ribosomal protein L32
+Macromolecule #67: 60S ribosomal protein L35a
+Macromolecule #68: 60S ribosomal protein L34
+Macromolecule #69: 60S ribosomal protein L35
+Macromolecule #70: 60S ribosomal protein L36
+Macromolecule #71: Ribosomal protein L37
+Macromolecule #72: 60S ribosomal protein L38
+Macromolecule #73: 60S ribosomal protein L39
+Macromolecule #74: Ubiquitin-60S ribosomal protein L40
+Macromolecule #75: 60S ribosomal protein L41
+Macromolecule #76: Ribosomal protein L36a
+Macromolecule #77: 60S ribosomal protein L37a
+Macromolecule #78: 60S ribosomal protein L28
+Macromolecule #83: 60S ribosomal protein L10a
+Macromolecule #84: ALA-ALA-LYS-ALA
+Macromolecule #85: MAGNESIUM ION
+Macromolecule #86: ZINC ION
+Macromolecule #87: water
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 Component:
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Grid | Model: C-flat-1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 3 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 10 sec. | |||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 10 K / Instrument: FEI VITROBOT MARK IV |
-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 / Number grids imaged: 1 / Number real images: 3644 / Average electron dose: 30.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 59000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |