9S3G
State 1 MAP3 RNA Pol II activated elongation complex with SETD2 and upstream hexasome
Summary for 9S3G
| Entry DOI | 10.2210/pdb9s3g/pdb |
| EMDB information | 54537 54538 54541 54542 |
| Descriptor | DNA-directed RNA polymerase subunit, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11-a, ... (34 entities in total) |
| Functional Keywords | rna pol ii activated elongation complex co-transcriptional h3k36me3 setd2, transcription |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 34 |
| Total formula weight | 1863695.45 |
| Authors | Walshe, J.L.,Ochmann, M.,Dienemann, C.,Cramer, P. (deposition date: 2025-07-24, release date: 2025-11-12) |
| Primary citation | Walshe, J.L.,Ochmann, M.,Neef, U.,Dybkov, O.,Dienemann, C.,Oberthur, C.,Zheenbekova, A.,Urlaub, H.,Cramer, P. Molecular mechanism of co-transcriptional H3K36 methylation by SETD2. Nat Commun, 16:9565-9565, 2025 Cited by PubMed Abstract: H3K36me3 is a hallmark of actively and recently transcribed genes and contributes to cellular memory and identity. The deposition of H3K36me3 occurs co-transcriptionally when the methyltransferase SETD2 associates with RNA polymerase II. Here we present three cryo-EM structures of SETD2 bound to RNA polymerase II elongation complexes at different states of nucleosome passage. Together with functional probing, our results suggest a 3-step mechanism of transcription-coupled H3K36me3 deposition. First, binding to the elongation factor SPT6 tethers the catalytic SET domain in proximity to the upstream DNA. Second, RNA polymerase II nucleosome passage leads to the transfer of a hexasome from downstream to upstream, poised for methylation. Finally, continued transcription leads to upstream nucleosome reassembly, partial dissociation of the histone chaperone FACT and sequential methylation of both H3 tails, completing H3K36me3 deposition of an upstream nucleosome after RNA polymerase II passage. PubMed: 41162378DOI: 10.1038/s41467-025-65439-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.4 Å) |
Structure validation
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