IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v558y2018i7709d10.1038_s41586-018-0193-0.html
   My bibliography  Save this article

Visualizing late states of human 40S ribosomal subunit maturation

Author

Listed:
  • Michael Ameismeier

    (University of Munich)

  • Jingdong Cheng

    (University of Munich)

  • Otto Berninghausen

    (University of Munich)

  • Roland Beckmann

    (University of Munich)

Abstract

The formation of eukaryotic ribosomal subunits extends from the nucleolus to the cytoplasm and entails hundreds of assembly factors. Despite differences in the pathways of ribosome formation, high-resolution structural information has been available only from fungi. Here we present cryo-electron microscopy structures of late-stage human 40S assembly intermediates, representing one state reconstituted in vitro and five native states that range from nuclear to late cytoplasmic. The earliest particles reveal the position of the biogenesis factor RRP12 and distinct immature rRNA conformations that accompany the formation of the 40S subunit head. Molecular models of the late-acting assembly factors TSR1, RIOK1, RIOK2, ENP1, LTV1, PNO1 and NOB1 provide mechanistic details that underlie their contribution to a sequential 40S subunit assembly. The NOB1 architecture displays an inactive nuclease conformation that requires rearrangement of the PNO1-bound 3′ rRNA, thereby coordinating the final rRNA folding steps with site 3 cleavage.

Suggested Citation

  • Michael Ameismeier & Jingdong Cheng & Otto Berninghausen & Roland Beckmann, 2018. "Visualizing late states of human 40S ribosomal subunit maturation," Nature, Nature, vol. 558(7709), pages 249-253, June.
  • Handle: RePEc:nat:nature:v:558:y:2018:i:7709:d:10.1038_s41586-018-0193-0
    DOI: 10.1038/s41586-018-0193-0
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41586-018-0193-0
    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/s41586-018-0193-0?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. Ken Ikeuchi & Nives Ivic & Robert Buschauer & Jingdong Cheng & Thomas Fröhlich & Yoshitaka Matsuo & Otto Berninghausen & Toshifumi Inada & Thomas Becker & Roland Beckmann, 2023. "Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    2. James C. Murphy & Elena M. Harrington & Sophie Schumann & Elton J. R. Vasconcelos & Timothy J. Mottram & Katherine L. Harper & Julie L. Aspden & Adrian Whitehouse, 2023. "Kaposi’s sarcoma-associated herpesvirus induces specialised ribosomes to efficiently translate viral lytic mRNAs," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Xiaomeng Liang & Mei-Qing Zuo & Yunyang Zhang & Ningning Li & Chengying Ma & Meng-Qiu Dong & Ning Gao, 2020. "Structural snapshots of human pre-60S ribosomal particles before and after nuclear export," Nature Communications, Nature, vol. 11(1), pages 1-14, 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:558:y:2018:i:7709:d:10.1038_s41586-018-0193-0. 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.