Structural highlights
7und is a 10 chain structure with sequence from Homo sapiens, Sus scrofa and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | Electron Microscopy, Resolution 3Å |
| Ligands: | , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
A0A7M4DUC2_PIG DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU004279]
Publication Abstract from PubMed
In eukaryotes, RNA polymerase (Pol) II transcribes chromatin and must move past nucleosomes, often resulting in nucleosome displacement. How Pol II unwraps the DNA from nucleosomes to allow transcription and how DNA rewraps to retain nucleosomes has been unclear. Here, we report the 3.0-angstrom cryo-electron microscopy structure of a mammalian Pol II-DSIF-SPT6-PAF1c-TFIIS-nucleosome complex stalled 54 base pairs within the nucleosome. The structure provides a mechanistic basis for nucleosome retention during transcription elongation where upstream DNA emerging from the Pol II cleft has rewrapped the proximal side of the nucleosome. The structure uncovers a direct role for Pol II and transcription elongation factors in nucleosome retention and explains how nucleosomes are retained to prevent the disruption of chromatin structure across actively transcribed genes.
Structural basis of nucleosome retention during transcription elongation.,Filipovski M, Soffers JHM, Vos SM, Farnung L Science. 2022 Jun 17;376(6599):1313-1316. doi: 10.1126/science.abo3851. Epub 2022 , Jun 16. PMID:35709268[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Filipovski M, Soffers JHM, Vos SM, Farnung L. Structural basis of nucleosome retention during transcription elongation. Science. 2022 Jun 17;376(6599):1313-1316. doi: 10.1126/science.abo3851. Epub 2022, Jun 16. PMID:35709268 doi:http://dx.doi.org/10.1126/science.abo3851
