IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v528y2015i7581d10.1038_nature16143.html
   My bibliography  Save this article

Molecular structures of unbound and transcribing RNA polymerase III

Author

Listed:
  • Niklas A. Hoffmann

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit)

  • Arjen J. Jakobi

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit
    European Molecular Biology Laboratory (EMBL), Hamburg Unit)

  • María Moreno-Morcillo

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit
    †Present addresses: Spanish National Cancer Research Centre (CNIO), Structural Biology and Biocomputing Programme, 28029 Madrid, Spain (M.M.-M.); Malopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A str, 30-387 Krakow, Poland (S.G.).)

  • Sebastian Glatt

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit
    †Present addresses: Spanish National Cancer Research Centre (CNIO), Structural Biology and Biocomputing Programme, 28029 Madrid, Spain (M.M.-M.); Malopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7A str, 30-387 Krakow, Poland (S.G.).)

  • Jan Kosinski

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit)

  • Wim J. H. Hagen

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit)

  • Carsten Sachse

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit)

  • Christoph W. Müller

    (European Molecular Biology Laboratory (EMBL), Structural and Computational Biology Unit)

Abstract

RNA polymerase III (Pol III), the largest eukaryote polymerase yet characterized, transcribes structured small non-coding RNAs; here cryo-electron microscopy structures of budding yeast Pol III allow building of an atomic-level model of the complete 17-subunit complex, both unbound and while elongating RNA.

Suggested Citation

  • Niklas A. Hoffmann & Arjen J. Jakobi & María Moreno-Morcillo & Sebastian Glatt & Jan Kosinski & Wim J. H. Hagen & Carsten Sachse & Christoph W. Müller, 2015. "Molecular structures of unbound and transcribing RNA polymerase III," Nature, Nature, vol. 528(7581), pages 231-236, December.
  • Handle: RePEc:nat:nature:v:528:y:2015:i:7581:d:10.1038_nature16143
    DOI: 10.1038/nature16143
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature16143
    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/nature16143?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. Haifeng Hou & Yan Li & Mo Wang & Aijun Liu & Zishuo Yu & Ke Chen & Dan Zhao & Yanhui Xu, 2021. "Structural insights into RNA polymerase III-mediated transcription termination through trapping poly-deoxythymidine," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    2. Saurabh Mishra & Shaina H. Hasan & Rima M. Sakhawala & Shereen Chaudhry & Richard J. Maraia, 2021. "Mechanism of RNA polymerase III termination-associated reinitiation-recycling conferred by the essential function of the N terminal-and-linker domain of the C11 subunit," Nature Communications, Nature, vol. 12(1), pages 1-16, 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. Joseph G. Beton & Thomas Mulvaney & Tristan Cragnolini & Maya Topf, 2024. "Cryo-EM structure and B-factor refinement with ensemble representation," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    5. Kevin Van Bortle & David P. Marciano & Qing Liu & Tristan Chou & Andrew M. Lipchik & Sanjay Gollapudi & Benjamin S. Geller & Emma Monte & Rohinton T. Kamakaka & Michael P. Snyder, 2022. "A cancer-associated RNA polymerase III identity drives robust transcription and expression of snaR-A noncoding RNA," Nature Communications, Nature, vol. 13(1), pages 1-17, 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:528:y:2015:i:7581:d:10.1038_nature16143. 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.