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6J4X

RNA polymerase II elongation complex bound with Elf1 and Spt4/5, stalled at SHL(-1) of the nucleosome (+1A)

Summary for 6J4X
Entry DOI10.2210/pdb6j4x/pdb
EMDB information0672
DescriptorDNA-directed RNA polymerase subunit, RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III, RNA polymerase II subunit B12.5, ... (24 entities in total)
Functional Keywordsnucleosome, chromatin, rna polymerase, transcription, transcription-rna-dna complex, transcription/rna/dna
Biological sourceKomagataella phaffii (strain GS115 / ATCC 20864) (Yeast)
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Total number of polymer chains26
Total formula weight876503.07
Authors
Ehara, H.,Kujirai, T.,Fujino, Y.,Shirouzu, M.,Kurumizaka, H.,Sekine, S. (deposition date: 2019-01-10, release date: 2019-02-20, Last modification date: 2024-03-27)
Primary citationEhara, H.,Kujirai, T.,Fujino, Y.,Shirouzu, M.,Kurumizaka, H.,Sekine, S.I.
Structural insight into nucleosome transcription by RNA polymerase II with elongation factors.
Science, 363:744-747, 2019
Cited by
PubMed Abstract: RNA polymerase II (RNAPII) transcribes chromosomal DNA that contains multiple nucleosomes. The nucleosome forms transcriptional barriers, and nucleosomal transcription requires several additional factors in vivo. We demonstrate that the transcription elongation factors Elf1 and Spt4/5 cooperatively lower the barriers and increase the RNAPII processivity in the nucleosome. The cryo-electron microscopy structures of the nucleosome-transcribing RNAPII elongation complexes (ECs) reveal that Elf1 and Spt4/5 reshape the EC downstream edge and intervene between RNAPII and the nucleosome. They facilitate RNAPII progression through superhelical location SHL(-1) by adjusting the nucleosome in favor of the forward progression. They suppress pausing at SHL(-5) by preventing the stable RNAPII-nucleosome interaction. Thus, the EC overcomes the nucleosomal barriers while providing a platform for various chromatin functions.
PubMed: 30733384
DOI: 10.1126/science.aav8912
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.3 Å)
Structure validation

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