+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-51134 | ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | human 40S ribosome bound by a SKI238-exosome complex | ||||||||||||||||||
Map data | |||||||||||||||||||
Sample |
| ||||||||||||||||||
Keywords | RNA-binding / RNA-degradation / cytoplasm / helicase / RIBOSOME | ||||||||||||||||||
Function / homology | Function and homology information DNA deamination / nucleolar exosome (RNase complex) / exoribonuclease II / exoribonuclease II activity / Dom34-Hbs1 complex / nuclear-transcribed mRNA catabolic process, no-go decay / U1 snRNA 3'-end processing / Ski complex / U5 snRNA 3'-end processing / TRAMP-dependent tRNA surveillance pathway ...DNA deamination / nucleolar exosome (RNase complex) / exoribonuclease II / exoribonuclease II activity / Dom34-Hbs1 complex / nuclear-transcribed mRNA catabolic process, no-go decay / U1 snRNA 3'-end processing / Ski complex / U5 snRNA 3'-end processing / TRAMP-dependent tRNA surveillance pathway / mRNA decay by 3' to 5' exoribonuclease / CUT catabolic process / cytoplasmic exosome (RNase complex) / U4 snRNA 3'-end processing / nuclear polyadenylation-dependent rRNA catabolic process / Cdc73/Paf1 complex / poly(A)-dependent snoRNA 3'-end processing / exosome (RNase complex) / nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay / nuclear exosome (RNase complex) / negative regulation of myeloid cell differentiation / exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / ATF4 activates genes in response to endoplasmic reticulum stress / histone mRNA catabolic process / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / rRNA catabolic process / 3'-5' RNA helicase activity / nuclear mRNA surveillance / positive regulation of isotype switching / ribosome disassembly / 7S RNA binding / : / negative regulation of endoplasmic reticulum unfolded protein response / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / protein tyrosine kinase inhibitor activity / positive regulation of respiratory burst involved in inflammatory response / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / mRNA 3'-UTR AU-rich region binding / positive regulation of gastrulation / nucleolus organization / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / isotype switching / IRE1-RACK1-PP2A complex / positive regulation of endodeoxyribonuclease activity / positive regulation of Golgi to plasma membrane protein transport / TNFR1-mediated ceramide production / negative regulation of RNA splicing / negative regulation of DNA repair / RNA catabolic process / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / supercoiled DNA binding / oxidized purine DNA binding / NF-kappaB complex / neural crest cell differentiation / ubiquitin-like protein conjugating enzyme binding / regulation of establishment of cell polarity / positive regulation of ubiquitin-protein transferase activity / negative regulation of phagocytosis / maturation of 5.8S rRNA / rRNA modification in the nucleus and cytosol / erythrocyte homeostasis / Formation of the ternary complex, and subsequently, the 43S complex / cytoplasmic side of rough endoplasmic reticulum membrane / laminin receptor activity / pigmentation / protein kinase A binding / negative regulation of ubiquitin protein ligase activity / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / KSRP (KHSRP) binds and destabilizes mRNA / Ribosomal scanning and start codon recognition / ion channel inhibitor activity / Translation initiation complex formation / nuclear chromosome / mammalian oogenesis stage / fibroblast growth factor binding / positive regulation of mitochondrial depolarization / activation-induced cell death of T cells / positive regulation of T cell receptor signaling pathway / negative regulation of peptidyl-serine phosphorylation / iron-sulfur cluster binding / negative regulation of Wnt signaling pathway / positive regulation of activated T cell proliferation / monocyte chemotaxis / Protein hydroxylation / regulation of cell division / Association of TriC/CCT with target proteins during biosynthesis / BH3 domain binding / cysteine-type endopeptidase activator activity involved in apoptotic process / mTORC1-mediated signalling / SARS-CoV-1 modulates host translation machinery / mRNA catabolic process / Peptide chain elongation / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / Selenocysteine synthesis / positive regulation of signal transduction by p53 class mediator / nuclear-transcribed mRNA catabolic process / Formation of a pool of free 40S subunits Similarity search - Function | ||||||||||||||||||
Biological species | Homo sapiens (human) / Cricket paralysis virus | ||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||||||||||||||
Authors | Koegel A / Keidel A / Loukeri MJ / Kuhn CC / Langer LM / Schaefer IB / Conti E | ||||||||||||||||||
Funding support | Germany, European Union, Denmark, 5 items
| ||||||||||||||||||
Citation | Journal: Nature / Year: 2024 Title: Structural basis of mRNA decay by the human exosome-ribosome supercomplex. Authors: Alexander Kögel / Achim Keidel / Matina-Jasemi Loukeri / Christopher C Kuhn / Lukas M Langer / Ingmar B Schäfer / Elena Conti / Abstract: The interplay between translation and mRNA decay is widespread in human cells. In quality-control pathways, exonucleolytic degradation of mRNA associated with translating ribosomes is mediated ...The interplay between translation and mRNA decay is widespread in human cells. In quality-control pathways, exonucleolytic degradation of mRNA associated with translating ribosomes is mediated largely by the cytoplasmic exosome, which includes the exoribonuclease complex EXO10 and the helicase complex SKI238 (refs. ). The helicase can extract mRNA from the ribosome and is expected to transfer it to the exoribonuclease core through a bridging factor, HBS1L3 (also known as SKI7), but the mechanisms of this molecular handover remain unclear. Here we reveal how human EXO10 is recruited by HBS1L3 (SKI7) to an active ribosome-bound SKI238 complex. We show that rather than a sequential handover, a direct physical coupling mechanism takes place, which culminates in the formation of a cytoplasmic exosome-ribosome supercomplex. Capturing the structure during active decay reveals a continuous path in which an RNA substrate threads from the 80S ribosome through the SKI2 helicase into the exoribonuclease active site of the cytoplasmic exosome complex. The SKI3 subunit of the complex directly binds to HBS1L3 (SKI7) and also engages a surface of the 40S subunit, establishing a recognition platform in collided disomes. Exosome and ribosome thus work together as a single structural and functional unit in co-translational mRNA decay, coordinating their activities in a transient supercomplex. | ||||||||||||||||||
History |
|
-Structure visualization
Supplemental images |
---|
-Downloads & links
-EMDB archive
Map data | emd_51134.map.gz | 71.4 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-51134-v30.xml emd-51134.xml | 74.5 KB 74.5 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_51134_fsc.xml | 29.4 KB | Display | FSC data file |
Images | emd_51134.png | 35.4 KB | ||
Masks | emd_51134_msk_1.map | 2.1 GB | Mask map | |
Filedesc metadata | emd-51134.cif.gz | 17.3 KB | ||
Others | emd_51134_additional_1.map.gz emd_51134_half_map_1.map.gz emd_51134_half_map_2.map.gz | 66.4 MB 1.5 GB 1.5 GB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51134 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51134 | HTTPS FTP |
-Validation report
Summary document | emd_51134_validation.pdf.gz | 750.5 KB | Display | EMDB validaton report |
---|---|---|---|---|
Full document | emd_51134_full_validation.pdf.gz | 750.1 KB | Display | |
Data in XML | emd_51134_validation.xml.gz | 37.5 KB | Display | |
Data in CIF | emd_51134_validation.cif.gz | 51.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51134 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51134 | HTTPS FTP |
-Related structure data
Related structure data | 9g8oMC 9g8mC 9g8nC 9g8pC 9g8qC 9g8rC M: atomic model generated by this map C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|---|
Related items in Molecule of the Month |
-Map
File | Download / File: emd_51134.map.gz / Format: CCP4 / Size: 2.1 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.8512 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Mask #1
File | emd_51134_msk_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Additional map: composite map human 40S ribosome bound to the...
File | emd_51134_additional_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | composite map human 40S ribosome bound to the SKI238 complex and the exosome | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #2
File | emd_51134_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #1
File | emd_51134_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Sample components
+Entire : human 40S ribosome bound by a SKI238-exosome complex
+Supramolecule #1: human 40S ribosome bound by a SKI238-exosome complex
+Macromolecule #1: Superkiller complex protein 3
+Macromolecule #2: WD repeat-containing protein 61
+Macromolecule #3: Exosome complex component RRP42
+Macromolecule #4: Exosome complex component CSL4
+Macromolecule #5: Exosome complex component RRP45
+Macromolecule #6: Exosome complex component RRP43
+Macromolecule #7: Exosome complex component RRP41
+Macromolecule #8: Exosome complex component RRP46
+Macromolecule #9: Helicase SKI2W
+Macromolecule #10: Isoform 2 of HBS1-like protein
+Macromolecule #11: Exosome complex component MTR3
+Macromolecule #12: Exosome complex component RRP40
+Macromolecule #13: Exosome complex component RRP4
+Macromolecule #15: 60S ribosomal protein L41
+Macromolecule #16: DIS3-like exonuclease 1
+Macromolecule #18: 40S ribosomal protein SA
+Macromolecule #19: 40S ribosomal protein S3a
+Macromolecule #20: 40S ribosomal protein S2
+Macromolecule #21: 40S ribosomal protein S3
+Macromolecule #22: 40S ribosomal protein S4, X isoform
+Macromolecule #23: 40S ribosomal protein S5
+Macromolecule #24: 40S ribosomal protein S6
+Macromolecule #25: 40S ribosomal protein S7
+Macromolecule #26: 40S ribosomal protein S8
+Macromolecule #27: 40S ribosomal protein S9
+Macromolecule #28: 40S ribosomal protein S10
+Macromolecule #29: 40S ribosomal protein S11
+Macromolecule #30: 40S ribosomal protein S12
+Macromolecule #31: 40S ribosomal protein S13
+Macromolecule #32: 40S ribosomal protein S14
+Macromolecule #33: 40S ribosomal protein S15
+Macromolecule #34: 40S ribosomal protein S16
+Macromolecule #35: 40S ribosomal protein S17
+Macromolecule #36: 40S ribosomal protein S18
+Macromolecule #37: 40S ribosomal protein S19
+Macromolecule #38: 40S ribosomal protein S20
+Macromolecule #39: 40S ribosomal protein S21
+Macromolecule #40: 40S ribosomal protein S15a
+Macromolecule #41: 40S ribosomal protein S23
+Macromolecule #42: 40S ribosomal protein S24
+Macromolecule #43: 40S ribosomal protein S25
+Macromolecule #44: 40S ribosomal protein S26
+Macromolecule #45: 40S ribosomal protein S27
+Macromolecule #46: 40S ribosomal protein S28
+Macromolecule #47: 40S ribosomal protein S29
+Macromolecule #48: 40S ribosomal protein S30
+Macromolecule #49: Ubiquitin
+Macromolecule #50: Receptor of activated protein C kinase 1
+Macromolecule #14: CrPV-IRES RNA
+Macromolecule #17: 18S ribosomal RNA
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
---|---|
Grid | Model: Quantifoil R2/1 / Mesh: 200 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE-PROPANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 64.2 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.6 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |