IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-18830-w.html
   My bibliography  Save this article

Analysis of translating mitoribosome reveals functional characteristics of translation in mitochondria of fungi

Author

Listed:
  • Yuzuru Itoh

    (Stockholm University
    Department of Medical Biochemistry and Biophysics, Karolinska Institutet)

  • Andreas Naschberger

    (Stockholm University)

  • Narges Mortezaei

    (Stockholm University)

  • Johannes M. Herrmann

    (University of Kaiserslautern)

  • Alexey Amunts

    (Stockholm University
    Department of Medical Biochemistry and Biophysics, Karolinska Institutet)

Abstract

Mitoribosomes are specialized protein synthesis machineries in mitochondria. However, how mRNA binds to its dedicated channel, and tRNA moves as the mitoribosomal subunit rotate with respect to each other is not understood. We report models of the translating fungal mitoribosome with mRNA, tRNA and nascent polypeptide, as well as an assembly intermediate. Nicotinamide adenine dinucleotide (NAD) is found in the central protuberance of the large subunit, and the ATPase inhibitory factor 1 (IF1) in the small subunit. The models of the active mitoribosome explain how mRNA binds through a dedicated protein platform on the small subunit, tRNA is translocated with the help of the protein mL108, bridging it with L1 stalk on the large subunit, and nascent polypeptide paths through a newly shaped exit tunnel involving a series of structural rearrangements. An assembly intermediate is modeled with the maturation factor Atp25, providing insight into the biogenesis of the mitoribosomal large subunit and translation regulation.

Suggested Citation

  • Yuzuru Itoh & Andreas Naschberger & Narges Mortezaei & Johannes M. Herrmann & Alexey Amunts, 2020. "Analysis of translating mitoribosome reveals functional characteristics of translation in mitochondria of fungi," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18830-w
    DOI: 10.1038/s41467-020-18830-w
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-18830-w
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-020-18830-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. Florent Waltz & Thalia Salinas-Giegé & Robert Englmeier & Herrade Meichel & Heddy Soufari & Lauriane Kuhn & Stefan Pfeffer & Friedrich Förster & Benjamin D. Engel & Philippe Giegé & Laurence Drouard &, 2021. "How to build a ribosome from RNA fragments in Chlamydomonas mitochondria," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    2. Victor Tobiasson & Ieva Berzina & Alexey Amunts, 2022. "Structure of a mitochondrial ribosome with fragmented rRNA in complex with membrane-targeting elements," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    3. Vivek Singh & Yuzuru Itoh & Samuel Del’Olio & Asem Hassan & Andreas Naschberger & Rasmus Kock Flygaard & Yuko Nobe & Keiichi Izumikawa & Shintaro Aibara & Juni Andréll & Paul C. Whitford & Antoni Barr, 2024. "Mitoribosome structure with cofactors and modifications reveals mechanism of ligand binding and interactions with L1 stalk," Nature Communications, Nature, vol. 15(1), pages 1-22, 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:11:y:2020:i:1:d:10.1038_s41467-020-18830-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.