IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v471y2011i7337d10.1038_nature09785.html
   My bibliography  Save this article

Structural basis of RNA polymerase II backtracking, arrest and reactivation

Author

Listed:
  • Alan C. M. Cheung

    (Center for Integrated Protein Science Munich, Ludwig-Maximilians-Universität München, Feodor-Lynen-Str. 25)

  • Patrick Cramer

    (Center for Integrated Protein Science Munich, Ludwig-Maximilians-Universität München, Feodor-Lynen-Str. 25)

Abstract

The to and fro of RNA polymerase RNA polymerase II (RNA pol II) moves forwards along the DNA strand during gene transcription, synthesizing messenger RNA as it goes. It can also move backwards and stall — a useful property for regulatory purposes or if it hits an obstacle such as a nucleosome. This arrested state is reactivated by transcription factor IIS (TFIIS). Now, the crystal structure of a backtracked yeast RNA pol II complex containing observable backtracked RNA has been determined at 3.3 Å resolution, as well as the structure of a backtracked complex containing TFIIS. The structures reveal possible mechanisms of transcriptional stalling and transcription reactivation.

Suggested Citation

  • Alan C. M. Cheung & Patrick Cramer, 2011. "Structural basis of RNA polymerase II backtracking, arrest and reactivation," Nature, Nature, vol. 471(7337), pages 249-253, March.
    • Handle: RePEc:nat:nature:v:471:y:2011:i:7337:d:10.1038_nature09785
    DOI: 10.1038/nature09785
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09785
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature09785?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Simona Pilotto & Michal Sýkora & Gwenny Cackett & Christopher Dulson & Finn Werner, 2024. "Structure of the recombinant RNA polymerase from African Swine Fever Virus," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Lisa-Marie Appel & Vedran Franke & Johannes Benedum & Irina Grishkovskaya & Xué Strobl & Anton Polyansky & Gregor Ammann & Sebastian Platzer & Andrea Neudolt & Anna Wunder & Lena Walch & Stefanie Kais, 2023. "The SPOC domain is a phosphoserine binding module that bridges transcription machinery with co- and post-transcriptional regulators," Nature Communications, Nature, vol. 14(1), pages 1-22, December.
    3. Phong Quoc Nguyen & Sonia Huecas & Amna Asif-Laidin & Adrián Plaza-Pegueroles & Beatrice Capuzzi & Noé Palmic & Christine Conesa & Joël Acker & Juan Reguera & Pascale Lesage & Carlos Fernández-Tornero, 2023. "Structural basis of Ty1 integrase tethering to RNA polymerase III for targeted retrotransposon integration," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    4. Lisa-Marie Appel & Vedran Franke & Melania Bruno & Irina Grishkovskaya & Aiste Kasiliauskaite & Tanja Kaufmann & Ursula E. Schoeberl & Martin G. Puchinger & Sebastian Kostrhon & Carmen Ebenwaldner & M, 2021. "PHF3 regulates neuronal gene expression through the Pol II CTD reader domain SPOC," Nature Communications, Nature, vol. 12(1), pages 1-24, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:471:y:2011:i:7337:d:10.1038_nature09785. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.