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Open data
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Basic information
Entry | Database: PDB / ID: 7aod | |||||||||
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Title | Schizosaccharomyces pombe RNA polymerase I (dimer) | |||||||||
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![]() | TRANSCRIPTION | |||||||||
Function / homology | ![]() RNA Polymerase I Transcription Initiation / RNA polymerase II transcribes snRNA genes / Processing of Capped Intron-Containing Pre-mRNA / 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 Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / mRNA Capping ...RNA Polymerase I Transcription Initiation / RNA polymerase II transcribes snRNA genes / Processing of Capped Intron-Containing Pre-mRNA / 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 Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / mRNA Capping / RNA Pol II CTD phosphorylation and interaction with CE / Estrogen-dependent gene expression / RNA polymerase II, holoenzyme / Formation of the Early Elongation Complex / RNA Polymerase I Promoter Escape / Formation of TC-NER Pre-Incision Complex / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / Transcriptional regulation by small RNAs / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / DNA-templated transcription elongation / termination of RNA polymerase I transcription / transcription initiation at RNA polymerase I promoter / transcription by RNA polymerase I / transcription by RNA polymerase III / transcription elongation by RNA polymerase I / RNA polymerase I complex / RNA polymerase III complex / RNA polymerase III activity / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / RNA polymerase I activity / RNA polymerase II activity / transcription initiation at RNA polymerase II promoter / ribonucleoside binding / DNA-directed RNA polymerase / transcription by RNA polymerase II / nucleic acid binding / protein dimerization activity / nucleolus / DNA binding / zinc ion binding / nucleus / metal ion binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.5 Å | |||||||||
![]() | Heiss, F. / Daiss, J. / Becker, P. / Engel, C. | |||||||||
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![]() | ![]() Title: Conserved strategies of RNA polymerase I hibernation and activation. Authors: Florian B Heiss / Julia L Daiß / Philipp Becker / Christoph Engel / ![]() Abstract: RNA polymerase (Pol) I transcribes the ribosomal RNA precursor in all eukaryotes. The mechanisms 'activation by cleft contraction' and 'hibernation by dimerization' are unique to the regulation of ...RNA polymerase (Pol) I transcribes the ribosomal RNA precursor in all eukaryotes. The mechanisms 'activation by cleft contraction' and 'hibernation by dimerization' are unique to the regulation of this enzyme, but structure-function analysis is limited to baker's yeast. To understand whether regulation by such strategies is specific to this model organism or conserved among species, we solve three cryo-EM structures of Pol I from Schizosaccharomyces pombe in different functional states. Comparative analysis of structural models derived from high-resolution reconstructions shows that activation is accomplished by a conserved contraction of the active center cleft. In contrast to current beliefs, we find that dimerization of the S. pombe polymerase is also possible. This dimerization is achieved independent of the 'connector' domain but relies on two previously undescribed interfaces. Our analyses highlight the divergent nature of Pol I transcription systems from their counterparts and suggest conservation of regulatory mechanisms among organisms. | |||||||||
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.3 MB | Display | ![]() |
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PDB format | ![]() | 1.1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 222.8 KB | Display | |
Data in CIF | ![]() | 328.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 11841MC ![]() 7aocC ![]() 7aoeC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
-DNA-directed RNA polymerase I subunit ... , 4 types, 8 molecules AMDPGSIU
#1: Protein | Mass: 189489.656 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: 972 / ATCC 24843 / References: UniProt: P15398, DNA-directed RNA polymerase #4: Protein | Mass: 17008.439 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: 972 / ATCC 24843 / References: UniProt: Q9P7P1 #7: Protein | Mass: 19406.354 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: 972 / ATCC 24843 / References: UniProt: O43036 #9: Protein | Mass: 13127.667 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: 972 / ATCC 24843 / References: UniProt: O94703 |
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-DNA-directed RNA polymerases I and III subunit ... , 2 types, 4 molecules COKW
#3: Protein | Mass: 39205.547 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: 972 / ATCC 24843 / References: UniProt: O94616 #11: Protein | Mass: 13734.478 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: 972 / ATCC 24843 / References: UniProt: Q09177 |
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-DNA-directed RNA polymerases I, II, and III subunit ... , 5 types, 10 molecules EQFRHTJVLX
#5: Protein | Mass: 23954.504 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: 972 / ATCC 24843 / References: UniProt: Q09191 #6: Protein | Mass: 15742.497 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: 972 / ATCC 24843 / References: UniProt: P36595 #8: Protein | Mass: 14317.318 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: 972 / ATCC 24843 / References: UniProt: Q92399 #10: Protein | Mass: 8286.801 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: 972 / ATCC 24843 / References: UniProt: O13877 #12: Protein | Mass: 7216.495 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: 972 / ATCC 24843 / References: UniProt: P48011 |
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-Protein / Non-polymers , 2 types, 14 molecules BN![](data/chem/img/ZN.gif)
![](data/chem/img/ZN.gif)
#13: Chemical | ChemComp-ZN / #2: Protein | Mass: 131854.969 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: 972 / ATCC 24843 / References: UniProt: Q9P7X8, DNA-directed RNA polymerase |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: S. pombe RNA polymerase I / Type: COMPLEX / Entity ID: #1-#12 / Source: NATURAL |
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Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 86.5 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
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CTF correction | Type: NONE | ||||||||||||||||||||||||
3D reconstruction | Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 17102 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 108.25 Å2 | ||||||||||||||||||||||||
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