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Yorodumi- PDB-9wms: Co-transcriptional histone H3K36 methylation complex containing R... -
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Basic information
| Entry | Database: PDB / ID: 9wms | |||||||||||||||||||||||||||||||||||||||
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| Title | Co-transcriptional histone H3K36 methylation complex containing RNA polymerase II elongation complex, Set2, and the upstream nucleosome. (temp115, type B) | |||||||||||||||||||||||||||||||||||||||
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Keywords | TRANSCRIPTION / chromatin / nucleosome | |||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationsnoRNA transcription by RNA polymerase II / sno(s)RNA transcription / negative regulation of antisense RNA transcription / negative regulation of transcription elongation by RNA polymerase I / regulation of transcription initiation by RNA polymerase II / sno(s)RNA 3'-end processing / negative regulation of reciprocal meiotic recombination / positive regulation of transcription elongation by RNA polymerase I / mating-type region heterochromatin / histone H3K36 dimethyltransferase activity ...snoRNA transcription by RNA polymerase II / sno(s)RNA transcription / negative regulation of antisense RNA transcription / negative regulation of transcription elongation by RNA polymerase I / regulation of transcription initiation by RNA polymerase II / sno(s)RNA 3'-end processing / negative regulation of reciprocal meiotic recombination / positive regulation of transcription elongation by RNA polymerase I / mating-type region heterochromatin / histone H3K36 dimethyltransferase activity / transcription antitermination factor activity, DNA binding / regulation of septum digestion after cytokinesis / RNA polymerase II C-terminal domain phosphoserine binding / [histone H3]-lysine36 N-trimethyltransferase / regulation of transcription-coupled nucleotide-excision repair / ascospore formation / triplex DNA binding / Cdc73/Paf1 complex / co-transcriptional lncRNA 3' end processing, cleavage and polyadenylation pathway / global genome nucleotide-excision repair / histone H3K36 trimethyltransferase activity / siRNA-mediated pericentric heterochromatin formation / regulation of mRNA 3'-end processing / DSIF complex / regulation of rRNA processing / intracellular mRNA localization / rDNA heterochromatin / rDNA binding / negative regulation of DNA recombination / intracellular phosphate ion homeostasis / rDNA heterochromatin formation / negative regulation of mitophagy / mRNA 3'-end processing / transcription elongation factor activity / chromatin-protein adaptor activity / transcription elongation-coupled chromatin remodeling / poly(A)+ mRNA export from nucleus / cellular response to stress / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / kinetochore assembly / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / RNA polymerase II complex binding / termination of RNA polymerase II transcription / DNA-templated transcription termination / 7-methylguanosine mRNA capping / termination of RNA polymerase I transcription / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / positive regulation of translational initiation / transcription initiation at RNA polymerase I promoter / transcription by RNA polymerase III / nuclear-transcribed mRNA catabolic process / mitotic metaphase chromosome alignment / negative regulation of tumor necrosis factor-mediated signaling pathway / pericentric heterochromatin / RNA polymerase II core promoter sequence-specific DNA binding / regulation of DNA-templated DNA replication initiation / termination of RNA polymerase III transcription / transcription initiation at RNA polymerase III promoter / RNA polymerase I complex / RNA polymerase III complex / transcription elongation by RNA polymerase I / negative regulation of megakaryocyte differentiation / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / protein localization to CENP-A containing chromatin / transcription by RNA polymerase I / Replacement of protamines by nucleosomes in the male pronucleus / nucleosome binding / CENP-A containing nucleosome / Packaging Of Telomere Ends / methylation / transcription-coupled nucleotide-excision repair / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / translesion synthesis / translation initiation factor binding / telomere organization / negative regulation of autophagy / ChAHP complex assembly / Deposition of new CENPA-containing nucleosomes at the centromere / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / RNA Polymerase I Promoter Opening / transcription initiation-coupled chromatin remodeling / Inhibition of DNA recombination at telomere / Assembly of the ORC complex at the origin of replication / FXIIa activates plasma kallikrein-kinin system / SUMOylation of chromatin organization proteins / DNA-templated transcription elongation / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / Meiotic synapsis / transcription elongation factor complex / regulation of DNA-templated transcription elongation / DNA methylation / Condensation of Prophase Chromosomes / Chromatin modifications during the maternal to zygotic transition (MZT) / HCMV Late Events / SIRT1 negatively regulates rRNA expression / NuRD complex assembly / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression Similarity search - Function | |||||||||||||||||||||||||||||||||||||||
| Biological species | Komagataella phaffii GS115 (fungus) Homo sapiens (human)synthetic construct (others) | |||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||||||||||||||||||||||||||||||||
Authors | Kujirai, T. / Ehara, H. / Ito, T. / Henmi, M. / Sekine, S. / Kurumizaka, H. | |||||||||||||||||||||||||||||||||||||||
| Funding support | Japan, 12items
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Citation | Journal: Sci Adv / Year: 2026Title: Structural basis of transcription-coupled H3K36 trimethylation by Set2 in coordination with FACT. Authors: Tomoya Kujirai / Haruhiko Ehara / Tomoko Ito / Masami Henmi / Eriko Oya / Takehiko Kobayashi / Shun-Ichi Sekine / Hitoshi Kurumizaka / ![]() Abstract: Trimethylation of the histone H3K36 residue (H3K36me3) plays an indispensable role in ensuring transcription fidelity by suppressing undesired cryptic transcription in chromatin. H3K36me3 ...Trimethylation of the histone H3K36 residue (H3K36me3) plays an indispensable role in ensuring transcription fidelity by suppressing undesired cryptic transcription in chromatin. H3K36me3 modification is accomplished by Set2/SETD2 during transcription elongation by the RNA polymerase II elongation complex (EC). Here, we found that Set2-mediated H3K36me3 deposition occurs on the nucleosome reassembling behind the EC. The histone chaperone FACT suppresses H3K36me3 deposition on the downstream nucleosome, thereby ensuring that Set2 targets specifically on the reassembling upstream nucleosome. Cryo-electron microscopy structures of the nucleosome-transcribing EC complexed with Set2 revealed that Set2 is anchored by the Spt6 subunit of the EC to capture both of the H3 N-terminal tails in a stepwise manner during the nucleosome reassembly process. Abrogation of the Set2-EC interaction leads to defective transcription-coupled H3K36me3 deposition. These insights elucidate the structure-based mechanism of transcription-coupled H3K36me3 deposition in chromatin. | |||||||||||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9wms.cif.gz | 1.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9wms.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9wms.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wm/9wms ftp://data.pdbj.org/pub/pdb/validation_reports/wm/9wms | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 66103MC ![]() 9wmtC ![]() 9wmuC ![]() 9wmvC ![]() 9wmwC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-DNA-directed RNA polymerase ... , 3 types, 3 molecules ABI
| #1: Protein | Mass: 194107.422 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Komagataella phaffii GS115 (fungus) / References: UniProt: C4R4Y0, DNA-directed RNA polymerase |
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| #2: Protein | Mass: 139746.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Komagataella phaffii GS115 (fungus) / References: UniProt: C4QZQ7, DNA-directed RNA polymerase |
| #9: Protein | Mass: 13612.320 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Komagataella phaffii GS115 (fungus) / References: UniProt: F2QPE6 |
-RNA polymerase II ... , 4 types, 4 molecules CDGK
| #3: Protein | Mass: 34216.293 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Komagataella phaffii GS115 (fungus) / References: UniProt: C4R7L2 |
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| #4: Protein | Mass: 20622.980 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Komagataella phaffii GS115 (fungus) / References: UniProt: C4R2U9 |
| #7: Protein | Mass: 18802.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Komagataella phaffii GS115 (fungus) / References: UniProt: C4R9A1 |
| #11: Protein | Mass: 13832.896 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Komagataella phaffii GS115 (fungus) / References: UniProt: C4R3Z5 |
-DNA-directed RNA polymerases I, II, and III subunit ... , 2 types, 2 molecules EH
| #5: Protein | Mass: 24962.680 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Komagataella phaffii GS115 (fungus) / References: UniProt: C4R3P8 |
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| #8: Protein | Mass: 16249.220 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Komagataella phaffii GS115 (fungus) / References: UniProt: C4R273 |
-Protein , 12 types, 16 molecules Fnqrsuvxaebfcgdh
| #6: Protein | Mass: 17803.588 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Komagataella phaffii GS115 (fungus) / References: UniProt: C4R1V1 | ||||||
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| #20: Protein | Mass: 46907.785 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Komagataella phaffii GS115 (fungus) / Gene: PAS_chr4_0349 / Production host: ![]() | ||||||
| #21: Protein | Mass: 124979.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Komagataella phaffii GS115 (fungus) / Gene: PAS_chr3_1035 / Production host: ![]() | ||||||
| #22: Protein | Mass: 62301.246 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Komagataella phaffii GS115 (fungus) / Gene: RTF1, PP7435_Chr1-1405 / Production host: ![]() | ||||||
| #23: Protein | Mass: 83724.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Komagataella phaffii GS115 (fungus) / Gene: PAS_chr1-4_0287 / Production host: ![]() References: UniProt: C4QY01, [histone H3]-lysine36 N-trimethyltransferase | ||||||
| #24: Protein | Mass: 52387.715 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Komagataella phaffii GS115 (fungus) / Gene: PAS_chr3_1154 / Production host: ![]() | ||||||
| #25: Protein | Mass: 46045.980 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Komagataella phaffii GS115 (fungus) / Gene: PAS_chr4_0902 / Production host: ![]() | ||||||
| #26: Protein | Mass: 44760.652 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Komagataella phaffii GS115 (fungus) / Gene: PAS_chr2-1_0674 / Production host: ![]() | ||||||
| #27: Protein | Mass: 15645.277 Da / Num. of mol.: 2 / Mutation: K36M Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: H3-3A, H3.3A, H3F3, H3F3A, PP781, H3-3B, H3.3B, H3F3B / Production host: ![]() #28: Protein | Mass: 11676.703 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human)Gene: H4C1, H4/A, H4FA, HIST1H4A, H4C2, H4/I, H4FI, HIST1H4B, H4C3, H4/G, H4FG, HIST1H4C, H4C4, H4/B, H4FB, HIST1H4D, H4C5, H4/J, H4FJ, HIST1H4E, H4C6, H4/C, H4FC, HIST1H4F, H4C8, H4/H, H4FH, ...Gene: H4C1, H4/A, H4FA, HIST1H4A, H4C2, H4/I, H4FI, HIST1H4B, H4C3, H4/G, H4FG, HIST1H4C, H4C4, H4/B, H4FB, HIST1H4D, H4C5, H4/J, H4FJ, HIST1H4E, H4C6, H4/C, H4FC, HIST1H4F, H4C8, H4/H, H4FH, HIST1H4H, H4C9, H4/M, H4FM, HIST1H4I, H4C11, H4/E, H4FE, HIST1H4J, H4C12, H4/D, H4FD, HIST1H4K, H4C13, H4/K, H4FK, HIST1H4L, H4C14, H4/N, H4F2, H4FN, HIST2H4, HIST2H4A, H4C15, H4/O, H4FO, HIST2H4B, H4C16, H4-16, HIST4H4 Production host: ![]() #29: Protein | Mass: 14447.825 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: H2AC4, H2AFM, HIST1H2AB, H2AC8, H2AFA, HIST1H2AE / Production host: ![]() #30: Protein | Mass: 14191.479 Da / Num. of mol.: 2 / Mutation: K121C-ubiquitination mimic Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HIST1H2BJ, H2BFR / Production host: ![]() |
-RNA polymerase subunit ABC10- ... , 2 types, 2 molecules JL
| #10: Protein | Mass: 8554.064 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Komagataella phaffii GS115 (fungus) / References: UniProt: C4R009 |
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| #12: Protein | Mass: 7862.048 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Komagataella phaffii GS115 (fungus) / References: UniProt: F2QMI1 |
-Transcription elongation factor ... , 4 types, 4 molecules MVWm
| #13: Protein | Mass: 12606.896 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Komagataella phaffii GS115 (fungus) / Gene: PAS_c121_0006 / Production host: ![]() |
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| #17: Protein | Mass: 12039.614 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Komagataella phaffii GS115 (fungus) / Gene: PAS_chr2-1_0350 / Production host: ![]() |
| #18: Protein | Mass: 101459.422 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Komagataella phaffii GS115 (fungus) / Gene: PAS_chr3_1136 / Production host: ![]() |
| #19: Protein | Mass: 173241.625 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Komagataella phaffii GS115 (fungus) / Gene: PAS_chr4_0308 / Production host: ![]() |
-DNA chain , 2 types, 2 molecules NT
| #14: DNA chain | Mass: 61264.703 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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| #16: DNA chain | Mass: 60987.176 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-RNA chain , 1 types, 1 molecules P
| #15: RNA chain | Mass: 6290.695 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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-Non-polymers , 3 types, 15 molecules 




| #31: Chemical | ChemComp-ZN / #32: Chemical | ChemComp-MG / | #33: Chemical | ChemComp-SAH / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | N |
-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: Co-transcriptional histone H3K36 methylation complex containing RNA polymerase II elongation complex, Set2, and the upstream nucleosome. (temp115, type B) Type: COMPLEX / Entity ID: #1-#30 / Source: MULTIPLE SOURCES | ||||||||||||
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| Molecular weight | Experimental value: NO | ||||||||||||
| Source (natural) |
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| Source (recombinant) |
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| Buffer solution | pH: 7.5 | ||||||||||||
| 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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 58 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.21.1_5286: / Category: model refinement |
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| CTF correction | Type: NONE |
| Symmetry | Point symmetry: C1 (asymmetric) |
| 3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 59019 / Symmetry type: POINT |
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About Yorodumi



Komagataella phaffii GS115 (fungus)
Homo sapiens (human)
Japan, 12items
Citation











PDBj








































































FIELD EMISSION GUN