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Open data
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Basic information
| Entry | Database: PDB / ID: 7ml1 | ||||||||||||||||||
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| Title | RNA polymerase II pre-initiation complex (PIC2) | ||||||||||||||||||
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Keywords | TRANSCRIPTION / PIC / TFIIH / ITC / RNA polymerase II | ||||||||||||||||||
| Function / homology | Function and homology information: / : / : / : / regulation of mitotic recombination / : / 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 / : / 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 / transcription factor TFIIIB complex / RNA polymerase II promoter clearance / positive regulation of mitotic recombination / transcription factor TFIIE complex / nucleotide-excision repair factor 3 complex / regulation of transcription by RNA polymerase III / nucleotide-excision repair, preincision complex assembly / DNA translocase activity / RNA polymerase I general transcription initiation factor binding / RNA Polymerase III Transcription Initiation From Type 1 Promoter / TFIIF-class transcription factor complex binding / transcriptional start site selection at RNA polymerase II promoter / transcription factor TFIIF complex / hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides / 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 / poly(A)+ mRNA export from nucleus / transcription factor TFIID complex / Processing of Capped Intron-Containing Pre-mRNA / RNA polymerase II general transcription initiation factor activity / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / Formation of TC-NER Pre-Incision Complex / TP53 Regulates Transcription of DNA Repair Genes / Estrogen-dependent gene expression / 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 I Promoter Escape / RNA Polymerase II Pre-transcription Events / ATPase activator activity / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / RNA polymerase II complex binding / Gap-filling DNA repair synthesis and ligation in TC-NER / DNA 3'-5' helicase / protein phosphatase activator activity / nucleolar large rRNA transcription by RNA polymerase I / Dual incision in TC-NER / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / 3'-5' DNA helicase activity / positive regulation of translational initiation / RNA polymerase II core promoter sequence-specific DNA binding / RNA polymerase II preinitiation complex assembly / RNA polymerase I complex / RNA polymerase III complex / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / transcription-coupled nucleotide-excision repair / translation initiation factor binding / TBP-class protein binding / DNA helicase activity / nucleotide-excision repair / positive regulation of transcription elongation by RNA polymerase II / transcription initiation at RNA polymerase II promoter / DNA-templated transcription initiation / P-body / transcription elongation by RNA polymerase II / ribonucleoside binding / disordered domain specific binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / transcription by RNA polymerase II / single-stranded DNA binding / double-stranded DNA binding / DNA-binding transcription factor binding / DNA helicase / nucleic acid binding / damaged DNA binding / RNA polymerase II-specific DNA-binding transcription factor binding / protein dimerization activity / single-stranded RNA binding / negative regulation of DNA-templated transcription / nucleotide binding / chromatin binding / regulation of transcription by RNA polymerase II / regulation of DNA-templated transcription / nucleolus / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity Similarity search - Function | ||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4 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 | 7ml1.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7ml1.ent.gz | 1.1 MB | Display | PDB format |
| PDBx/mmJSON format | 7ml1.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ml/7ml1 ftp://data.pdbj.org/pub/pdb/validation_reports/ml/7ml1 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 23905MC ![]() 7meiC ![]() 7mk9C ![]() 7mkaC ![]() 7ml0C ![]() 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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Components
+Protein , 6 types, 6 molecules 123OFM
+General transcription and DNA repair factor IIH subunit ... , 3 types, 3 molecules 465
+General transcription and DNA repair factor IIH helicase subunit ... , 2 types, 2 molecules 07
+DNA chain , 2 types, 2 molecules NT
+DNA-directed RNA polymerase ... , 7 types, 7 molecules ABCDGIK
+DNA-directed RNA polymerases I, II, and III subunit ... , 2 types, 2 molecules EH
+DNA-directed RNA polymerases II subunit ... , 2 types, 2 molecules JL
+Transcription initiation factor IIF subunit ... , 2 types, 2 molecules QR
+Transcription initiation factor IIA ... , 2 types, 2 molecules UV
+Transcription initiation factor IIE subunit ... , 2 types, 2 molecules WX
+Non-polymers , 3 types, 21 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 | |||||||||||||||||||||||||||||||||||
| Specimen support | Grid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R0.6/1 | |||||||||||||||||||||||||||||||||||
| 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: 4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 33150 Details: the final map is a composite of 3 individually 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
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