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TitleCryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2.
Journal, issue, pagesCommun Biol, Vol. 4, Issue 1, Page 606, Year 2021
Publish dateMay 21, 2021
AuthorsIsaac Fianu / Christian Dienemann / Shintaro Aibara / Sandra Schilbach / Patrick Cramer /
PubMed AbstractNuclear 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. ...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.
External linksCommun Biol / PubMed:34021257 / PubMed Central
MethodsEM (single particle)
Resolution2.8 Å
Structure data

12087

7b7u

EMDB-12087, PDB-7b7u:
Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • sus scrofa domesticus (domestic pig)
  • homo sapiens (human)
KeywordsTRANSCRIPTION / RPAP2 / RNA polymerase II / Nuclear import

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