7XN7

RNA polymerase II elongation complex containing Spt4/5, Elf1, Spt6, Spn1 and Paf1C

This is a non-PDB format compatible entry.

Summary for 7XN7

• Entry DOI: 10.2210/pdb7xn7/pdb
• EMDB information: 33313
• 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, ... (27 entities in total)
• Functional Keywords: chromatin, nucleosome, transcription
• Biological source: Komagataella phaffii; More
• Total number of polymer chains: 25
• Total formula weight: 1316114.01

Authors

Ehara, H.,Kujirai, T.,Shirouzu, M.,Kurumizaka, H.,Sekine, S. (deposition date: 2022-04-28, release date: 2022-09-07, Last modification date: 2024-07-03)

Primary citation

Ehara, H.,Kujirai, T.,Shirouzu, M.,Kurumizaka, H.,Sekine, S.I.
Structural basis of nucleosome disassembly and reassembly by RNAPII elongation complex with FACT.
Science, 377:eabp9466-eabp9466, 2022

PubMed Abstract: During gene transcription, RNA polymerase II (RNAPII) traverses nucleosomes in chromatin, but the mechanism has remained elusive. Using cryo-electron microscopy, we obtained structures of the RNAPII elongation complex (EC) passing through a nucleosome in the presence of the transcription elongation factors Spt6, Spn1, Elf1, Spt4/5, and Paf1C and the histone chaperone FACT (facilitates chromatin transcription). The structures show snapshots of EC progression on DNA mediating downstream nucleosome disassembly, followed by its reassembly upstream of the EC, which is facilitated by FACT. FACT dynamically adapts to successively occurring subnucleosome intermediates, forming an interface with the EC. Spt6, Spt4/5, and Paf1C form a "cradle" at the EC DNA-exit site and support the upstream nucleosome reassembly. These structures explain the mechanism by which the EC traverses nucleosomes while maintaining the chromatin structure and epigenetic information.

PubMed: 35981082
DOI: 10.1126/science.abp9466

Experimental method

ELECTRON MICROSCOPY (3.1 Å)