IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v9y2018i1d10.1038_s41467-018-07783-w.html
   My bibliography  Save this article

RNA helicases mediate structural transitions and compositional changes in pre-ribosomal complexes

Author

Listed:
  • Lukas Brüning

    (University Medical Center Göttingen)

  • Philipp Hackert

    (University Medical Center Göttingen)

  • Roman Martin

    (University Medical Center Göttingen)

  • Jimena Davila Gallesio

    (University Medical Center Göttingen)

  • Gerald Ryan R. Aquino

    (University Medical Center Göttingen)

  • Henning Urlaub

    (Bioanalytical Mass Spectrometry
    University Medical Center Göttingen)

  • Katherine E. Sloan

    (University Medical Center Göttingen)

  • Markus T. Bohnsack

    (University Medical Center Göttingen
    Georg-August-University)

Abstract

Production of eukaryotic ribosomal subunits is a highly dynamic process; pre-ribosomes undergo numerous structural rearrangements that establish the architecture present in mature complexes and serve as key checkpoints, ensuring the fidelity of ribosome assembly. Using in vivo crosslinking, we here identify the pre-ribosomal binding sites of three RNA helicases. Our data support roles for Has1 in triggering release of the U14 snoRNP, a critical event during early 40S maturation, and in driving assembly of domain I of pre-60S complexes. Binding of Mak5 to domain II of pre-60S complexes promotes recruitment of the ribosomal protein Rpl10, which is necessary for subunit joining and ribosome function. Spb4 binds to a molecular hinge at the base of ES27 facilitating binding of the export factor Arx1, thereby promoting pre-60S export competence. Our data provide important insights into the driving forces behind key structural remodelling events during ribosomal subunit assembly.

Suggested Citation

  • Lukas Brüning & Philipp Hackert & Roman Martin & Jimena Davila Gallesio & Gerald Ryan R. Aquino & Henning Urlaub & Katherine E. Sloan & Markus T. Bohnsack, 2018. "RNA helicases mediate structural transitions and compositional changes in pre-ribosomal complexes," Nature Communications, Nature, vol. 9(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07783-w
    DOI: 10.1038/s41467-018-07783-w
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-018-07783-w
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-018-07783-w?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
    ---><---

    Citations

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


    Cited by:

    1. Gerald Ryan R. Aquino & Philipp Hackert & Nicolai Krogh & Kuan-Ting Pan & Mariam Jaafar & Anthony K. Henras & Henrik Nielsen & Henning Urlaub & Katherine E. Bohnsack & Markus T. Bohnsack, 2021. "The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly," Nature Communications, Nature, vol. 12(1), pages 1-16, 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:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07783-w. 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.