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Yorodumi- PDB-9wmt: Co-transcriptional histone H3K36 methylation complex containing R... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9wmt | |||||||||||||||||||||||||||||||||||||||
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| Title | Co-transcriptional histone H3K36 methylation complex containing RNA polymerase II elongation complex, Set2, and the upstream nucleosome. (temp115, type A) | |||||||||||||||||||||||||||||||||||||||
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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 / regulation of transcription initiation by RNA polymerase II / negative regulation of reciprocal meiotic recombination / negative regulation of transcription elongation by RNA polymerase I / sno(s)RNA 3'-end processing / histone H3K36 dimethyltransferase activity / positive regulation of transcription elongation by RNA polymerase I / mating-type region heterochromatin ...snoRNA transcription by RNA polymerase II / sno(s)RNA transcription / negative regulation of antisense RNA transcription / regulation of transcription initiation by RNA polymerase II / negative regulation of reciprocal meiotic recombination / negative regulation of transcription elongation by RNA polymerase I / sno(s)RNA 3'-end processing / histone H3K36 dimethyltransferase activity / positive regulation of transcription elongation by RNA polymerase I / mating-type region heterochromatin / regulation of septum digestion after cytokinesis / transcription antitermination factor activity, DNA binding / RNA polymerase II C-terminal domain phosphoserine binding / ascospore formation / [histone H3]-lysine36 N-trimethyltransferase / co-transcriptional lncRNA 3' end processing, cleavage and polyadenylation pathway / regulation of transcription-coupled nucleotide-excision repair / triplex DNA binding / Cdc73/Paf1 complex / histone H3K36 trimethyltransferase activity / siRNA-mediated pericentric heterochromatin formation / regulation of mRNA 3'-end processing / Barr body / RNA polymerase I core binding / DSIF complex / regulation of rRNA processing / RNA polymerase I general transcription initiation factor binding / intracellular mRNA localization / negative regulation of chromosome condensation / rDNA binding / rDNA heterochromatin / pericentric heterochromatin formation / negative regulation of DNA recombination / inner kinetochore / RPB4-RPB7 complex / muscle cell differentiation / DNA-templated transcription elongation / intracellular phosphate ion homeostasis / snRNP binding / transcription elongation-coupled chromatin remodeling / mRNA 3'-end processing / chromatin-protein adaptor activity / U4 snRNA binding / oocyte maturation / transcription elongation factor activity / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / regulation of DNA-templated DNA replication initiation / nucleosomal DNA binding / termination of RNA polymerase II transcription / poly(A)+ mRNA export from nucleus / termination of RNA polymerase III transcription / nucleus organization / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / cellular response to stress / negative regulation of mitophagy / transcription initiation at RNA polymerase III promoter / termination of RNA polymerase I transcription / transcription initiation at RNA polymerase I promoter / spliceosomal complex assembly / RNA polymerase II complex binding / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / positive regulation of translational initiation / nuclear-transcribed mRNA catabolic process / U5 snRNA binding / spermatid development / 7-methylguanosine mRNA capping / U2 snRNA binding / U6 snRNA binding / single fertilization / negative regulation of tumor necrosis factor-mediated signaling pathway / subtelomeric heterochromatin formation / translation elongation factor activity / RNA polymerase I complex / RNA polymerase III complex / transcription elongation by RNA polymerase I / U1 snRNA binding / pericentric heterochromatin / RNA polymerase II core promoter sequence-specific DNA binding / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / nucleosome binding / transcription by RNA polymerase I / negative regulation of megakaryocyte differentiation / translesion synthesis / protein localization to CENP-A containing chromatin / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / transcription-coupled nucleotide-excision repair / translation initiation factor binding / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / embryo implantation / Deposition of new CENPA-containing nucleosomes at the centromere / positive regulation of autophagy / telomere organization / 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 Similarity search - Function | |||||||||||||||||||||||||||||||||||||||
| Biological species | Komagataella phaffii GS115 (fungus) Homo sapiens (human)synthetic construct (others) | |||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.59 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 | 9wmt.cif.gz | 1.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9wmt.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9wmt.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wm/9wmt ftp://data.pdbj.org/pub/pdb/validation_reports/wm/9wmt | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 66104MC ![]() 9wmsC ![]() 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 A) Type: COMPLEX / Entity ID: #1-#30 / Source: RECOMBINANT | ||||||||||||
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| Molecular weight | Experimental value: NO | ||||||||||||
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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: 3.59 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 35823 / Symmetry type: POINT |
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About Yorodumi



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








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FIELD EMISSION GUN