8A40

Structure of mammalian Pol II-TFIIS elongation complex

Summary for 8A40

• Entry DOI: 10.2210/pdb8a40/pdb
• EMDB information: 15129
• Descriptor: DNA-directed RNA polymerase subunit, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11-a, ... (18 entities in total)
• Functional Keywords: chromatin, rna polymerase ii, nucleosome, tfiis, transcription, elongation
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 16
• Total formula weight: 594086.32

Authors

Farnung, L.,Ochmann, M.,Garg, G.,Vos, S.M.,Cramer, P. (deposition date: 2022-06-09, release date: 2023-08-23, Last modification date: 2024-11-13)

Primary citation

Farnung, L.,Ochmann, M.,Garg, G.,Vos, S.M.,Cramer, P.
Structure of a backtracked hexasomal intermediate of nucleosome transcription.
Mol.Cell, 82:3126-3134.e7, 2022

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 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.

PubMed: 35858621
DOI: 10.1016/j.molcel.2022.06.027

Experimental method

ELECTRON MICROSCOPY (3 Å)