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29VF

RNA polymerase II initially transcribing complex with a 2-nt RNA and the +1 nucleosome

This is a non-PDB format compatible entry.
Summary for 29VF
Entry DOI10.2210/pdb29vf/pdb
EMDB information57390
DescriptorGeneral transcription and DNA repair factor IIH helicase subunit XPB, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase II subunit RPB3, ... (38 entities in total)
Functional Keywordsrna polymerase ii, transcription
Biological sourceHomo sapiens (human)
More
Total number of polymer chains39
Total formula weight1504432.34
Authors
Zhan, Y.,Abril-Garrido, J.,Dienemann, C.,Cramer, P. (deposition date: 2026-04-09, release date: 2026-07-22, Last modification date: 2026-09-02)
Primary citationZhan, Y.,Abril-Garrido, J.,Grabbe, F.,Seweryn, P.,Neef, U.,Dienemann, C.,Cramer, P.
The +1 nucleosome functions in RNA Pol II transcription initiation and the transition to elongation.
Mol.Cell, 86:2939-, 2026
Cited by
PubMed Abstract: Transcription initiation by RNA polymerase II (RNA Pol II) occurs next to a +1 nucleosome, which is positioned downstream of the transcription start site (TSS). The +1 nucleosome influences pre-initiation complex (PIC) assembly and RNA Pol II pausing, but its function in transcription initiation and the transition to elongation remains unclear. Here, we investigate the transcription initiation-elongation transition in vitro using DNA templates containing a +1 nucleosome and present cryo-electron microscopy (cryo-EM) structures of five intermediate states. First, after PIC assembly, ATP binding to TFIIH enables the +1 nucleosome to evict TFIID from the PIC. Following DNA opening, the +1 nucleosome stimulates TFIIH translocase activity and initial RNA synthesis. Finally, after DNA bubble rewinding, the +1 nucleosome removes TFIIH from the early elongation complex for promoter escape. Our findings show that the +1 nucleosome not only acts passively in PIC assembly and RNA Pol II pausing but rather has active functions during the initiation-elongation transition of transcription.
PubMed: 42480520
DOI: 10.1016/j.molcel.2026.06.042
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.5 Å)
Structure validation

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PDB entries from 2026-09-09

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