9rze | pdb_00009rze

State 2 MAP 3 RNA Pol II activated elongation complex with SETD2 bound to proximal upstream H3

spinqualitylabelsall models 9rze, resolution 8.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9rze is a 10 chain structure with sequence from Sus scrofa and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 8.53Å Ligands: MG, SEP, TPO, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A287ADR4_PIG Publication Abstract from PubMed 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. Molecular mechanism of co-transcriptional H3K36 methylation by SETD2.,Walshe JL, Ochmann M, Neef U, Dybkov O, Dienemann C, Oberthur C, Zheenbekova A, Urlaub H, Cramer P Nat Commun. 2025 Oct 29;16(1):9565. doi: 10.1038/s41467-025-65439-y. PMID:41162378 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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