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Yorodumi- EMDB-19022: Structure of Sen1-ADP.BeF3 bound RNA Polymerase II pre-terminatio... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-19022 | |||||||||
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Title | Structure of Sen1-ADP.BeF3 bound RNA Polymerase II pre-termination complex | |||||||||
Map data | ||||||||||
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Keywords | RNA Polymerase II / Pol II / termination / Sen1 / GENE REGULATION | |||||||||
Function / homology | Function and homology information negative regulation of transcription elongation by RNA polymerase I / transcription termination site sequence-specific DNA binding / negative regulation of flocculation / 5'-3' DNA/RNA helicase activity / Nrd1 complex / mating-type region heterochromatin / positive regulation of transcription elongation by RNA polymerase I / sno(s)RNA 3'-end processing / regulation of transcription-coupled nucleotide-excision repair / DNA-templated DNA replication maintenance of fidelity ...negative regulation of transcription elongation by RNA polymerase I / transcription termination site sequence-specific DNA binding / negative regulation of flocculation / 5'-3' DNA/RNA helicase activity / Nrd1 complex / mating-type region heterochromatin / positive regulation of transcription elongation by RNA polymerase I / sno(s)RNA 3'-end processing / regulation of transcription-coupled nucleotide-excision repair / DNA-templated DNA replication maintenance of fidelity / regulation of rRNA processing / snRNA processing / RNA polymerase I core binding / DSIF complex / intracellular mRNA localization / rDNA heterochromatin / rDNA binding / RNA polymerase I general transcription initiation factor binding / RPB4-RPB7 complex / snRNP binding / U4 snRNA binding / mRNA 3'-end processing / RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / RNA Polymerase III Transcription Initiation From Type 2 Promoter / tRNA processing / transcription elongation-coupled chromatin remodeling / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / TP53 Regulates Transcription of DNA Repair Genes / termination of RNA polymerase II transcription / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA-templated transcription / RNA Polymerase II Pre-transcription Events / termination of RNA polymerase III transcription / Formation of TC-NER Pre-Incision Complex / transcription initiation at RNA polymerase III promoter / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / termination of RNA polymerase I transcription / RNA Polymerase I Promoter Escape / nucleolar large rRNA transcription by RNA polymerase I / spliceosomal complex assembly / RNA polymerase II complex binding / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription by RNA polymerase I / transcription initiation at RNA polymerase I promoter / Estrogen-dependent gene expression / nuclear-transcribed mRNA catabolic process / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / transcription by RNA polymerase III / RNA polymerase II activity / Dual incision in TC-NER / 7-methylguanosine mRNA capping / transcription elongation by RNA polymerase I / transcription-coupled nucleotide-excision repair / tRNA transcription by RNA polymerase III / U5 snRNA binding / RNA polymerase I activity / RNA polymerase I complex / RNA polymerase III complex / positive regulation of translational initiation / translesion synthesis / U2 snRNA binding / RNA polymerase II, core complex / U6 snRNA binding / positive regulation of autophagy / U1 snRNA binding / translation initiation factor binding / cell redox homeostasis / negative regulation of autophagy / transcription initiation-coupled chromatin remodeling / transcription elongation factor complex / maturation of SSU-rRNA / replication fork / DNA-templated transcription initiation / small-subunit processome / transcription initiation at RNA polymerase II promoter / positive regulation of transcription elongation by RNA polymerase II / DNA-templated transcription termination / transcription elongation by RNA polymerase II / P-body / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / heterochromatin formation / ribonucleoside binding / kinetochore / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / cytoplasmic stress granule / mRNA processing / rRNA processing / peroxisome / ribosome biogenesis / chromatin organization / single-stranded DNA binding Similarity search - Function | |||||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) / Human immunodeficiency virus 2 | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.3 Å | |||||||||
Authors | Rengachari S / Lidscreiber M / Cramer P | |||||||||
Funding support | Germany, 1 items
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Citation | Journal: Nat Struct Mol Biol / Year: 2024 Title: Mechanism of polyadenylation-independent RNA polymerase II termination. Authors: Srinivasan Rengachari / Thomas Hainthaler / Christiane Oberthuer / Michael Lidschreiber / Patrick Cramer / Abstract: The mechanisms underlying the initiation and elongation of RNA polymerase II (Pol II) transcription are well-studied, whereas termination remains poorly understood. Here we analyze the mechanism of ...The mechanisms underlying the initiation and elongation of RNA polymerase II (Pol II) transcription are well-studied, whereas termination remains poorly understood. Here we analyze the mechanism of polyadenylation-independent Pol II termination mediated by the yeast Sen1 helicase. Cryo-electron microscopy structures of two pretermination intermediates show that Sen1 binds to Pol II and uses its adenosine triphosphatase activity to pull on exiting RNA in the 5' direction. This is predicted to push Pol II forward, induce an unstable hypertranslocated state and destabilize the transcription bubble, thereby facilitating termination. This mechanism of transcription termination may be widely used because it is conceptually conserved in the bacterial transcription system. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_19022.map.gz | 103.3 MB | EMDB map data format | |
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Header (meta data) | emd-19022-v30.xml emd-19022.xml | 43.9 KB 43.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_19022_fsc.xml | 12.8 KB | Display | FSC data file |
Images | emd_19022.png | 96.8 KB | ||
Masks | emd_19022_msk_1.map | 178 MB | Mask map | |
Filedesc metadata | emd-19022.cif.gz | 12.5 KB | ||
Others | emd_19022_half_map_1.map.gz emd_19022_half_map_2.map.gz | 141.4 MB 141.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-19022 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-19022 | HTTPS FTP |
-Validation report
Summary document | emd_19022_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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Full document | emd_19022_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | emd_19022_validation.xml.gz | 20 KB | Display | |
Data in CIF | emd_19022_validation.cif.gz | 26.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19022 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19022 | HTTPS FTP |
-Related structure data
Related structure data | 8rapMC 8ramC 8ranC 8raoC 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_19022.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.05 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_19022_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_19022_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_19022_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Tertiary complex of RNA Polymerase II with elongation factors Elf...
+Supramolecule #1: Tertiary complex of RNA Polymerase II with elongation factors Elf...
+Supramolecule #2: DNA-directed RNA polymerase II
+Supramolecule #3: Transcription elongation factors
+Supramolecule #4: RNA
+Supramolecule #5: DNA
+Macromolecule #1: DNA-directed RNA polymerase II subunit RPB1
+Macromolecule #2: DNA-directed RNA polymerase II subunit RPB2
+Macromolecule #3: DNA-directed RNA polymerase II subunit RPB3
+Macromolecule #4: DNA-directed RNA polymerase II subunit RPB4
+Macromolecule #5: DNA-directed RNA polymerases I, II, and III subunit RPABC1
+Macromolecule #6: DNA-directed RNA polymerases I, II, and III subunit RPABC2
+Macromolecule #7: DNA-directed RNA polymerase II subunit RPB7
+Macromolecule #8: DNA-directed RNA polymerases I, II, and III subunit RPABC3
+Macromolecule #9: DNA-directed RNA polymerase II subunit RPB9
+Macromolecule #10: DNA-directed RNA polymerases I, II, and III subunit RPABC5
+Macromolecule #11: DNA-directed RNA polymerase II subunit RPB11
+Macromolecule #12: DNA-directed RNA polymerases I, II, and III subunit RPABC4
+Macromolecule #13: Transcription elongation factor 1
+Macromolecule #15: Helicase SEN1
+Macromolecule #18: Transcription elongation factor SPT4
+Macromolecule #19: Transcription elongation factor SPT5
+Macromolecule #14: Non-template strand
+Macromolecule #17: Template strand
+Macromolecule #16: RNA
+Macromolecule #20: ZINC ION
+Macromolecule #21: MAGNESIUM ION
+Macromolecule #22: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #23: BERYLLIUM TRIFLUORIDE ION
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.02 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: 2.5 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Initial model |
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Refinement | Protocol: OTHER | ||||||||||
Output model | PDB-8rap: |