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-Structure paper
Title | Structure of a backtracked hexasomal intermediate of nucleosome transcription. |
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Journal, issue, pages | Mol Cell, Vol. 82, Issue 17, Page 3126-33134.e7, Year 2022 |
Publish date | Sep 1, 2022 |
Authors | Lucas Farnung / Moritz Ochmann / Gaurika Garg / Seychelle M Vos / Patrick Cramer / |
PubMed Abstract | During gene transcription, RNA polymerase II (RNA Pol II) passes nucleosomes with the help of various elongation factors. Here, we show that RNA Pol II achieves efficient nucleosome passage when the ...During gene transcription, RNA polymerase II (RNA Pol II) passes nucleosomes with the help of various elongation factors. Here, we show that RNA Pol II achieves efficient nucleosome passage when the human elongation factors DSIF, PAF1 complex (PAF), RTF1, SPT6, and TFIIS are present. The cryo-EM structure of an intermediate of the nucleosome passage shows a partially unraveled hexasome that lacks the proximal H2A-H2B dimer and interacts with the RNA Pol II jaw, DSIF, and the CTR9trestle helix. RNA Pol II adopts a backtracked state with the RNA 3' end dislodged from the active site and bound in the RNA Pol II pore. Additional structures and biochemical data show that human TFIIS enters the RNA Pol II pore and stimulates the cleavage of the backtracked RNA and nucleosome passage. |
External links | Mol Cell / PubMed:35858621 |
Methods | EM (single particle) |
Resolution | 3.0 - 6.0 Å |
Structure data | EMDB-15127, PDB-8a3y: EMDB-15129, PDB-8a40: EMDB-51079: Structure of activated elongation complex with hexasome (Pol II focused) EMDB-51081: Structure of mammalian Pol II-DSIF-SPT6-PAF1-TFIIS-hexasome elongation complex (Hexasome focused map) |
Chemicals | ChemComp-ZN: ChemComp-MG: |
Source |
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Keywords | TRANSCRIPTION / chromatin / rna polymerase II / nucleosome / TFIIS / elongation |