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9WMV

Co-transcriptional histone H3K36 methylation complex containing RNA polymerase II elongation complex, Set2, and the upstream nucleosome. (temp130, type B)

This is a non-PDB format compatible entry.
Summary for 9WMV
Entry DOI10.2210/pdb9wmv/pdb
EMDB information66106
DescriptorDNA-directed RNA polymerase subunit, RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III, RNA polymerase II subunit B12.5, ... (33 entities in total)
Functional Keywordschromatin, nucleosome, transcription
Biological sourceKomagataella phaffii GS115
More
Total number of polymer chains34
Total formula weight1512309.83
Authors
Kujirai, T.,Ehara, H.,Ito, T.,Henmi, M.,Sekine, S.,Kurumizaka, H. (deposition date: 2025-09-03, release date: 2025-12-24, Last modification date: 2026-03-04)
Primary citationKujirai, T.,Ehara, H.,Ito, T.,Henmi, M.,Oya, E.,Kobayashi, T.,Sekine, S.I.,Kurumizaka, H.
Structural basis of transcription-coupled H3K36 trimethylation by Set2 in coordination with FACT.
Sci Adv, 12:eaed1952-eaed1952, 2026
Cited by
PubMed Abstract: 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.
PubMed: 41604494
DOI: 10.1126/sciadv.aed1952
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.66 Å)
Structure validation

250059

PDB entries from 2026-03-04

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