6J4X
RNA polymerase II elongation complex bound with Elf1 and Spt4/5, stalled at SHL(-1) of the nucleosome (+1A)
Summary for 6J4X
Entry DOI | 10.2210/pdb6j4x/pdb |
EMDB information | 0672 |
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, ... (24 entities in total) |
Functional Keywords | nucleosome, chromatin, rna polymerase, transcription, transcription-rna-dna complex, transcription/rna/dna |
Biological source | Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) More |
Total number of polymer chains | 26 |
Total formula weight | 876503.07 |
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 citation | Ehara, 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: 30733384DOI: 10.1126/science.aav8912 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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