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7XSE

RNA polymerase II elongation complex transcribing a nucleosome (EC42)

This is a non-PDB format compatible entry.
Summary for 7XSE
Entry DOI10.2210/pdb7xse/pdb
EMDB information33424
DescriptorDNA-directed RNA polymerase subunit, RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III, RNA polymerase II subunit B12.5, ... (31 entities in total)
Functional Keywordschromatin, nucleosome, transcription
Biological sourceKomagataella phaffii
More
Total number of polymer chains33
Total formula weight1428084.63
Authors
Ehara, H.,Kujirai, T.,Shirouzu, M.,Kurumizaka, H.,Sekine, S. (deposition date: 2022-05-13, release date: 2022-09-07, Last modification date: 2024-07-03)
Primary citationEhara, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

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