Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2
2021 | journal article; research paper. A publication with affiliation to the University of Göttingen.
Jump to: Cite & Linked | Documents & Media | Details | Version history
Documents & Media
s42003-021-02088-z-1.pdf1.03 MBAdobe PDF42003_2021_2088_MOESM1_ESM.pdf457.75 kBAdobe PDF42003_2021_2088_MOESM2_ESM.docx4.53 MBMicrosoft Word XML42003_2021_2088_MOESM3_ESM.pdf285.07 kBAdobe PDF
Details
- Authors
- Fianu, Isaac; Dienemann, Christian; Aibara, Shintaro; Schilbach, Sandra; Cramer, Patrick
- Abstract
- Nuclear import of RNA polymerase II (Pol II) involves the conserved factor RPAP2. Here we report the cryo-electron microscopy (cryo-EM) structure of mammalian Pol II in complex with human RPAP2 at 2.8 Å resolution. The structure shows that RPAP2 binds between the jaw domains of the polymerase subunits RPB1 and RPB5. RPAP2 is incompatible with binding of downstream DNA during transcription and is displaced upon formation of a transcription pre-initiation complex.
- Issue Date
- 2021
- Journal
- Communications Biology
- Project
- EXC 2067: Multiscale Bioimaging
- Organization
- Max-Planck-Institut für biophysikalische Chemie
- Working Group
- RG Cramer
- ISSN
- 2399-3642
- Language
- English
