Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2

Commun Biol. 2021 May 21;4(1):606. doi: 10.1038/s42003-021-02088-z.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cryoelectron Microscopy / methods*
  • DNA / metabolism*
  • Humans
  • Mammals
  • Protein Conformation
  • RNA Polymerase II / chemistry*
  • RNA Polymerase II / genetics
  • RNA Polymerase II / metabolism*
  • Transcription, Genetic*

Substances

  • Carrier Proteins
  • RPAP2 protein, human
  • DNA
  • RNA Polymerase II