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

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 subuni...

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Autores principales: Fianu, Isaac, Dienemann, Christian, Aibara, Shintaro, Schilbach, Sandra, Cramer, Patrick
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8140126/
https://www.ncbi.nlm.nih.gov/pubmed/34021257
http://dx.doi.org/10.1038/s42003-021-02088-z
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author Fianu, Isaac
Dienemann, Christian
Aibara, Shintaro
Schilbach, Sandra
Cramer, Patrick
author_facet Fianu, Isaac
Dienemann, Christian
Aibara, Shintaro
Schilbach, Sandra
Cramer, Patrick
author_sort Fianu, Isaac
collection PubMed
description 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.
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spelling pubmed-81401262021-06-03 Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2 Fianu, Isaac Dienemann, Christian Aibara, Shintaro Schilbach, Sandra Cramer, Patrick Commun Biol Article 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. Nature Publishing Group UK 2021-05-21 /pmc/articles/PMC8140126/ /pubmed/34021257 http://dx.doi.org/10.1038/s42003-021-02088-z Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Fianu, Isaac
Dienemann, Christian
Aibara, Shintaro
Schilbach, Sandra
Cramer, Patrick
Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2
title Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2
title_full Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2
title_fullStr Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2
title_full_unstemmed Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2
title_short Cryo-EM structure of mammalian RNA polymerase II in complex with human RPAP2
title_sort cryo-em structure of mammalian rna polymerase ii in complex with human rpap2
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8140126/
https://www.ncbi.nlm.nih.gov/pubmed/34021257
http://dx.doi.org/10.1038/s42003-021-02088-z
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