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

Isaac Fianu, Christian Dienemann, Shintaro Aibara, S. Schilbach, Patrick Cramer

2021Communications Biology21 citationsDOIOpen Access PDF

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.

Topics & Concepts

RNA polymerase IITranscription (linguistics)Transcription factor II DPolymeraseRNA polymerase ICell biologyMolecular biologyTranscription factor II FRNA polymeraseBiologyChemistryBiophysicsRNADNAGeneticsRNA-dependent RNA polymeraseGene expressionGenePromoterLinguisticsPhilosophyRNA Research and SplicingRNA and protein synthesis mechanismsRNA modifications and cancer
Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2 | Litcius