+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-14803 | |||||||||
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Title | Structure of an ALYREF-exon junction complex hexamer | |||||||||
Map data | Locally sharpened ALYREF(55-183)-EJC-RNA map | |||||||||
Sample |
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Function / homology | Function and homology information exon-exon junction subcomplex mago-y14 / negative regulation of selenocysteine incorporation / regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / transcription export complex / cellular response to selenite ion / C5-methylcytidine-containing RNA reader activity / exon-exon junction complex / selenocysteine insertion sequence binding / regulation of translation at postsynapse, modulating synaptic transmission / negative regulation of excitatory postsynaptic potential ...exon-exon junction subcomplex mago-y14 / negative regulation of selenocysteine incorporation / regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / transcription export complex / cellular response to selenite ion / C5-methylcytidine-containing RNA reader activity / exon-exon junction complex / selenocysteine insertion sequence binding / regulation of translation at postsynapse, modulating synaptic transmission / negative regulation of excitatory postsynaptic potential / Z-decay: degradation of maternal mRNAs by zygotically expressed factors / regulation of mRNA processing / Deadenylation of mRNA / Transport of the SLBP independent Mature mRNA / Transport of the SLBP Dependant Mature mRNA / poly(A) binding / M-decay: degradation of maternal mRNAs by maternally stored factors / mRNA 3'-end processing / Transport of Mature mRNA Derived from an Intronless Transcript / U2-type catalytic step 1 spliceosome / embryonic cranial skeleton morphogenesis / RNA export from nucleus / Transport of Mature mRNA derived from an Intron-Containing Transcript / RNA Polymerase II Transcription Termination / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / exploration behavior / regulation of alternative mRNA splicing, via spliceosome / maltose binding / maltose transport / maltodextrin transmembrane transport / associative learning / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / mRNA export from nucleus / ribonucleoprotein complex binding / RNA stem-loop binding / cellular response to brain-derived neurotrophic factor stimulus / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / RNA splicing / positive regulation of translation / response to organic cyclic compound / ISG15 antiviral mechanism / mRNA processing / Regulation of expression of SLITs and ROBOs / mRNA splicing, via spliceosome / osteoblast differentiation / rRNA processing / regulation of translation / outer membrane-bounded periplasmic space / postsynapse / RNA helicase activity / negative regulation of translation / RNA helicase / nuclear speck / mRNA binding / neuronal cell body / glutamatergic synapse / dendrite / nucleolus / ATP hydrolysis activity / RNA binding / extracellular exosome / nucleoplasm / ATP binding / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.4 Å | |||||||||
Authors | Pacheco-Fiallos FB / Vorlaender MK / Plaschka C | |||||||||
Funding support | European Union, 2 items
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Citation | Journal: Nature / Year: 2023 Title: mRNA recognition and packaging by the human transcription-export complex. Authors: Belén Pacheco-Fiallos / Matthias K Vorländer / Daria Riabov-Bassat / Laura Fin / Francis J O'Reilly / Farja I Ayala / Ulla Schellhaas / Juri Rappsilber / Clemens Plaschka / Abstract: Newly made mRNAs are processed and packaged into mature ribonucleoprotein complexes (mRNPs) and are recognized by the essential transcription-export complex (TREX) for nuclear export. However, the ...Newly made mRNAs are processed and packaged into mature ribonucleoprotein complexes (mRNPs) and are recognized by the essential transcription-export complex (TREX) for nuclear export. However, the mechanisms of mRNP recognition and three-dimensional mRNP organization are poorly understood. Here we report cryo-electron microscopy and tomography structures of reconstituted and endogenous human mRNPs bound to the 2-MDa TREX complex. We show that mRNPs are recognized through multivalent interactions between the TREX subunit ALYREF and mRNP-bound exon junction complexes. Exon junction complexes can multimerize through ALYREF, which suggests a mechanism for mRNP organization. Endogenous mRNPs form compact globules that are coated by multiple TREX complexes. These results reveal how TREX may simultaneously recognize, compact and protect mRNAs to promote their packaging for nuclear export. The organization of mRNP globules provides a framework to understand how mRNP architecture facilitates mRNA biogenesis and export. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_14803.map.gz | 9.1 MB | EMDB map data format | |
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Header (meta data) | emd-14803-v30.xml emd-14803.xml | 24.3 KB 24.3 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_14803_fsc.xml | 10.5 KB | Display | FSC data file |
Images | emd_14803.png | 170.9 KB | ||
Masks | emd_14803_msk_1.map | 125 MB | Mask map | |
Others | emd_14803_additional_1.map.gz emd_14803_additional_2.map.gz emd_14803_half_map_1.map.gz emd_14803_half_map_2.map.gz | 117.9 MB 62.1 MB 115.8 MB 115.8 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-14803 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-14803 | HTTPS FTP |
-Related structure data
Related structure data | 7znjMC 7znkC 7znlC C: citing same article (ref.) M: atomic model generated by this map |
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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_14803.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Annotation | Locally sharpened ALYREF(55-183)-EJC-RNA map | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.945 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_14803_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: Globally sharpened ALYREF(55-183)-EJC-RNA map
File | emd_14803_additional_1.map | ||||||||||||
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Annotation | Globally sharpened ALYREF(55-183)-EJC-RNA map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Unsharpened ALYREF(55-183)-EJC-RNA map
File | emd_14803_additional_2.map | ||||||||||||
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Annotation | Unsharpened ALYREF(55-183)-EJC-RNA map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: ALYREF(55-183)-EJC-RNA half map
File | emd_14803_half_map_1.map | ||||||||||||
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Annotation | ALYREF(55-183)-EJC-RNA half map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: ALYREF(55-183)-EJC-RNA half map
File | emd_14803_half_map_2.map | ||||||||||||
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Annotation | ALYREF(55-183)-EJC-RNA half map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Hexameric complex between the TREX subunit ALYREF and the exon ju...
Entire | Name: Hexameric complex between the TREX subunit ALYREF and the exon junction complex |
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Components |
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-Supramolecule #1: Hexameric complex between the TREX subunit ALYREF and the exon ju...
Supramolecule | Name: Hexameric complex between the TREX subunit ALYREF and the exon junction complex type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: #1-#5 Details: Assembled with truncated MBP-tagged ALYREF (residues 55-183) |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 650 KDa |
-Macromolecule #1: Eukaryotic initiation factor 4A-III, N-terminally processed
Macromolecule | Name: Eukaryotic initiation factor 4A-III, N-terminally processed type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 43.819367 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MTKVEFETSE EVDVTPTFDT MGLREDLLRG IYAYGFEKPS AIQQRAIKQI IKGRDVIAQS QSGTGKTATF SISVLQCLDI QVRETQALI LAPTRELAVQ IQKGLLALGD YMNVQCHACI GGTNVGEDIR KLDYGQHVVA GTPGRVFDMI RRRSLRTRAI K MLVLDEAD ...String: MTKVEFETSE EVDVTPTFDT MGLREDLLRG IYAYGFEKPS AIQQRAIKQI IKGRDVIAQS QSGTGKTATF SISVLQCLDI QVRETQALI LAPTRELAVQ IQKGLLALGD YMNVQCHACI GGTNVGEDIR KLDYGQHVVA GTPGRVFDMI RRRSLRTRAI K MLVLDEAD EMLNKGFKEQ IYDVYRYLPP ATQVVLISAT LPHEILEMTN KFMTDPIRIL VKRDELTLEG IKQFFVAVER EE WKFDTLC DLYDTLTITQ AVIFCNTKRK VDWLTEKMRE ANFTVSSMHG DMPQKERESI MKEFRSGASR VLISTDVWAR GLD VPQVSL IINYDLPNNR ELYIHRIGRS GRYGRKGVAI NFVKNDDIRI LRDIEQYYST QIDEMP |
-Macromolecule #2: Protein mago nashi homolog
Macromolecule | Name: Protein mago nashi homolog / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 17.189625 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MESDFYLRYY VGHKGKFGHE FLEFEFRPDG KLRYANNSNY KNDVMIRKEA YVHKSVMEEL KRIIDDSEIT KEDDALWPPP DRVGRQELE IVIGDEHISF TTSKIGSLID VNQSKDPEGL RVFYYLVQDL KCLVFSLIGL HFKIKPI |
-Macromolecule #3: RNA-binding protein 8A
Macromolecule | Name: RNA-binding protein 8A / type: protein_or_peptide / ID: 3 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 10.370525 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: GPQRSVEGWI LFVTGVHEEA TEEDIHDKFA EYGEIKNIHL NLDRRTGYLK GYTLVEYETY KEAQAAMEGL NGQDLMGQPI SVDWCFVRG PP |
-Macromolecule #4: Maltose/maltodextrin-binding periplasmic protein,THO complex subunit 4
Macromolecule | Name: Maltose/maltodextrin-binding periplasmic protein,THO complex subunit 4 type: protein_or_peptide / ID: 4 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 57.598855 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MQLSHHHHHH HHHHSSGMKI EEGKLVIWIN GDKGYNGLAE VGKKFEKDTG IKVTVEHPDK LEEKFPQVAA TGDGPDIIFW AHDRFGGYA QSGLLAEITP DKAFQDKLYP FTWDAVRYNG KLIAYPIAVE ALSLIYNKDL LPNPPKTWEE IPALDKELKA K GKSALMFN ...String: MQLSHHHHHH HHHHSSGMKI EEGKLVIWIN GDKGYNGLAE VGKKFEKDTG IKVTVEHPDK LEEKFPQVAA TGDGPDIIFW AHDRFGGYA QSGLLAEITP DKAFQDKLYP FTWDAVRYNG KLIAYPIAVE ALSLIYNKDL LPNPPKTWEE IPALDKELKA K GKSALMFN LQEPYFTWPL IAADGGYAFK YENGKYDIKD VGVDNAGAKA GLTFLVDLIK NKHMNADTDY SIAEAAFNKG ET AMTINGP WAWSNIDTSK VNYGVTVLPT FKGQPSKPFV GVLSAGINAA SPNKELAKEF LENYLLTDEG LEAVNKDKPL GAV ALKSYE EELAKDPRIA ATMENAQKGE IMPNIPQMSA FWYAVRTAVI NAASGRQTVD EALKDAQTSS GLEVLFQGPG SSGI RNRPA IARGAAGGGG RNRPAPYSRP KQLPDKWQHD LFDSGFGGGA GVETGGKLLV SNLDFGVSDA DIQELFAEFG TLKKA AVHY DRSGRSLGTA DVHFERKADA LKAMKQYNGV PLDGRPMNIQ LVT |
-Macromolecule #5: RNA
Macromolecule | Name: RNA / type: rna / ID: 5 / Number of copies: 6 |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 1.792037 KDa |
Sequence | String: UUUUUU |
-Macromolecule #6: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 6 / Number of copies: 6 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #7: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
Macromolecule | Name: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / type: ligand / ID: 7 / Number of copies: 6 / Formula: ANP |
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Molecular weight | Theoretical: 506.196 Da |
Chemical component information | ChemComp-ANP: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 1.7 mg/mL |
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Buffer | pH: 7.9 |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.6 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |