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Journal Article

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

MPS-Authors
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Fianu,  I.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Dienemann,  C.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Aibara,  S.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Schilbach,  S.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Cramer,  P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Fianu, I., Dienemann, C., Aibara, S., Schilbach, S., & Cramer, P. (2021). Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2. Communications Biology, 4: 606. doi:10.1038/s42003-021-02088-z.


Cite as: https://hdl.handle.net/21.11116/0000-0008-A650-2
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.