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Open data
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Basic information
| Entry | Database: PDB / ID: 7ml0 | ||||||||||||||||||
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| Title | RNA polymerase II pre-initiation complex (PIC1) | ||||||||||||||||||
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Keywords | TRANSCRIPTION / PIC / TFIIH / ITC / RNA polymerase II | ||||||||||||||||||
| Function / homology | Function and homology information: / : / : / : / regulation of mitotic recombination / RNA polymerase II complex recruiting activity / transcription open complex formation at RNA polymerase II promoter / TFIIA-class transcription factor complex binding / RNA polymerase III transcription regulatory region sequence-specific DNA binding / : ...: / : / : / : / regulation of mitotic recombination / RNA polymerase II complex recruiting activity / transcription open complex formation at RNA polymerase II promoter / TFIIA-class transcription factor complex binding / RNA polymerase III transcription regulatory region sequence-specific DNA binding / : / TFIIH-class transcription factor complex binding / RNA polymerase III preinitiation complex assembly / RNA polymerase II promoter clearance / transcription factor TFIIIB complex / positive regulation of mitotic recombination / nucleotide-excision repair factor 3 complex / RNA polymerase I general transcription initiation factor binding / transcription factor TFIIE complex / nucleotide-excision repair, preincision complex assembly / DNA translocase activity / regulation of transcription by RNA polymerase III / TFIIF-class transcription factor complex binding / transcriptional start site selection at RNA polymerase II promoter / hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides / transcription factor TFIIF complex / transcription factor TFIIA complex / RNA polymerase I preinitiation complex assembly / transcription factor TFIIH core complex / transcription factor TFIIH holo complex / cyclin-dependent protein serine/threonine kinase activator activity / DNA binding, bending / transcription preinitiation complex / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase III Transcription Initiation From Type 2 Promoter / poly(A)+ mRNA export from nucleus / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / DNA 3'-5' helicase / TP53 Regulates Transcription of DNA Repair Genes / 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 II general transcription initiation factor activity / transcription factor TFIID complex / RNA Polymerase II Pre-transcription Events / 3'-5' DNA helicase activity / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / Formation of TC-NER Pre-Incision Complex / RNA Polymerase I Promoter Escape / nucleolar large rRNA transcription by RNA polymerase I / Gap-filling DNA repair synthesis and ligation in TC-NER / RNA polymerase II complex binding / Estrogen-dependent gene expression / ATPase activator activity / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / positive regulation of translational initiation / Dual incision in TC-NER / protein phosphatase activator activity / RNA polymerase I complex / RNA polymerase III complex / RNA polymerase II core promoter sequence-specific DNA binding / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / RNA polymerase II preinitiation complex assembly / translation initiation factor binding / transcription-coupled nucleotide-excision repair / DNA helicase activity / TBP-class protein binding / nucleotide-excision repair / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / P-body / DNA-templated transcription initiation / positive regulation of transcription elongation by RNA polymerase II / ribonucleoside binding / DNA-directed RNA polymerase / disordered domain specific binding / DNA-directed RNA polymerase activity / single-stranded DNA binding / double-stranded DNA binding / transcription regulator complex / DNA-binding transcription factor binding / DNA helicase / damaged DNA binding / nucleic acid binding / RNA polymerase II-specific DNA-binding transcription factor binding / transcription by RNA polymerase II / single-stranded RNA binding / protein dimerization activity / nucleotide binding / negative regulation of DNA-templated transcription / DNA-templated transcription / chromatin binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / nucleolus / positive regulation of transcription by RNA polymerase II Similarity search - Function | ||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | ||||||||||||||||||
Authors | Yang, C. / Fujiwara, R. / Kim, H.J. / Gorbea Colon, J.J. / Steimle, S. / Garcia, B.A. / Murakami, K. | ||||||||||||||||||
| Funding support | United States, 5items
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Citation | Journal: Mol Cell / Year: 2022Title: Structural visualization of de novo transcription initiation by Saccharomyces cerevisiae RNA polymerase II. Authors: Chun Yang / Rina Fujiwara / Hee Jong Kim / Pratik Basnet / Yunye Zhu / Jose J Gorbea Colón / Stefan Steimle / Benjamin A Garcia / Craig D Kaplan / Kenji Murakami / ![]() Abstract: Previous structural studies of the initiation-elongation transition of RNA polymerase II (pol II) transcription have relied on the use of synthetic oligonucleotides, often artificially discontinuous ...Previous structural studies of the initiation-elongation transition of RNA polymerase II (pol II) transcription have relied on the use of synthetic oligonucleotides, often artificially discontinuous to capture pol II in the initiating state. Here, we report multiple structures of initiation complexes converted de novo from a 33-subunit yeast pre-initiation complex (PIC) through catalytic activities and subsequently stalled at different template positions. We determine that PICs in the initially transcribing complex (ITC) can synthesize a transcript of ∼26 nucleotides before transitioning to an elongation complex (EC) as determined by the loss of general transcription factors (GTFs). Unexpectedly, transition to an EC was greatly accelerated when an ITC encountered a downstream EC stalled at promoter proximal regions and resulted in a collided head-to-end dimeric EC complex. Our structural analysis reveals a dynamic state of TFIIH, the largest of GTFs, in PIC/ITC with distinct functional consequences at multiple steps on the pathway to elongation. | ||||||||||||||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7ml0.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7ml0.ent.gz | 1.1 MB | Display | PDB format |
| PDBx/mmJSON format | 7ml0.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7ml0_validation.pdf.gz | 1 MB | Display | wwPDB validaton report |
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| Full document | 7ml0_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 7ml0_validation.xml.gz | 239.7 KB | Display | |
| Data in CIF | 7ml0_validation.cif.gz | 372.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ml/7ml0 ftp://data.pdbj.org/pub/pdb/validation_reports/ml/7ml0 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 23904MC ![]() 7meiC ![]() 7mk9C ![]() 7mkaC ![]() 7ml1C ![]() 7ml2C ![]() 7ml3C ![]() 7ml4C M: map data used to model this data C: citing same article ( |
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| Similar structure data | |
| EM raw data | EMPIAR-10865 (Title: Structural visualization of de novo initiation of RNA polymerase II transcriptionData size: 14.3 TB Data #1: raw micrographs for PIC + ITC maps [micrographs - multiframe] Data #2: raw micrographs for EC+EC map [micrographs - multiframe]) |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
+DNA-directed RNA polymerase ... , 9 types, 9 molecules ABCDGIK14
+DNA-directed RNA polymerases I, II, and III subunit ... , 2 types, 2 molecules EH
+Protein , 5 types, 5 molecules FMO23
+DNA-directed RNA polymerases II subunit ... , 2 types, 2 molecules JL
+Transcription initiation factor IIF subunit ... , 2 types, 2 molecules QR
+Transcription initiation factor IIE subunit ... , 2 types, 2 molecules WX
+DNA chain , 2 types, 2 molecules TN
+General transcription and DNA repair factor IIH helicase subunit ... , 2 types, 2 molecules 07
+General transcription and DNA repair factor IIH subunit ... , 2 types, 2 molecules 65
+Non-polymers , 3 types, 19 molecules 




+Details
-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
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| Buffer solution | pH: 7.6 | |||||||||||||||||||||||||||||||||||
| 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: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 45 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||
| 3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 137466 Details: Final map is a composite of 3 separately refined domains. Symmetry type: POINT | ||||||||||||||||||||
| Atomic model building | Space: REAL | ||||||||||||||||||||
| Atomic model building | PDB-ID: 5OQJ Accession code: 5OQJ / Source name: PDB / Type: experimental model |
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About Yorodumi






United States, 5items
Citation
UCSF Chimera
























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