6A5L

RNA polymerase II elongation complex stalled at SHL(-1) of the nucleosome, with foreign DNA

Summary for 6A5L

• Entry DOI: 10.2210/pdb6a5l/pdb
• EMDB information: 6980
• Descriptor: DNA-directed RNA polymerase subunit, RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III, RNA polymerase II subunit B12.5, ... (23 entities in total)
• Functional Keywords: nucleosome, chromatin, rna polymerase, transcription, transcription-rna-dna complex, transcription/rna/dna
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 25
• Total formula weight: 774560.04

Authors

Kujirai, T.,Ehara, H.,Fujino, Y.,Shirouzu, M.,Sekine, S.,Kurumizaka, H. (deposition date: 2018-06-24, release date: 2018-10-03, Last modification date: 2024-03-27)

Primary citation

Kujirai, T.,Ehara, H.,Fujino, Y.,Shirouzu, M.,Sekine, S.I.,Kurumizaka, H.
Structural basis of the nucleosome transition during RNA polymerase II passage.
Science, 362:595-598, 2018

PubMed Abstract: Genomic DNA forms chromatin, in which the nucleosome is the repeating unit. The mechanism by which RNA polymerase II (RNAPII) transcribes the nucleosomal DNA remains unclear. Here we report the cryo-electron microscopy structures of RNAPII-nucleosome complexes in which RNAPII pauses at the superhelical locations SHL(-6), SHL(-5), SHL(-2), and SHL(-1) of the nucleosome. RNAPII pauses at the major histone-DNA contact sites, and the nucleosome interactions with the RNAPII subunits stabilize the pause. These structures reveal snapshots of nucleosomal transcription, in which RNAPII gradually tears DNA from the histone surface while preserving the histone octamer. The nucleosomes in the SHL(-1) complexes are bound to a "foreign" DNA segment, which might explain the histone transfer mechanism. These results provide the foundations for understanding chromatin transcription and epigenetic regulation.

PubMed: 30287617
DOI: 10.1126/science.aau9904

Experimental method

ELECTRON MICROSCOPY (5.6 Å)