IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v10y2019i1d10.1038_s41467-019-13579-3.html
   My bibliography  Save this article

Oxidation and alkylation stresses activate ribosome-quality control

Author

Listed:
  • Liewei L. Yan

    (Washington University in St. Louis)

  • Carrie L. Simms

    (Washington University in St. Louis)

  • Fionn McLoughlin

    (Washington University in St. Louis)

  • Richard D. Vierstra

    (Washington University in St. Louis)

  • Hani S. Zaher

    (Washington University in St. Louis)

Abstract

Oxidation and alkylation of nucleobases are known to disrupt their base-pairing properties within RNA. It is, however, unclear whether organisms have evolved general mechanism(s) to deal with this damage. Here we show that the mRNA-surveillance pathway of no-go decay and the associated ribosome-quality control are activated in response to nucleobase alkylation and oxidation. Our findings reveal that these processes are important for clearing chemically modified mRNA and the resulting aberrant-protein products. In the absence of Xrn1, the level of damaged mRNA significantly increases. Furthermore, deletion of LTN1 results in the accumulation of protein aggregates in the presence of oxidizing and alkylating agents. This accumulation is accompanied by Hel2-dependent regulatory ubiquitylation of ribosomal proteins. Collectively, our data highlight the burden of chemically damaged mRNA on cellular homeostasis and suggest that organisms evolved mechanisms to counter their accumulation.

Suggested Citation

  • Liewei L. Yan & Carrie L. Simms & Fionn McLoughlin & Richard D. Vierstra & Hani S. Zaher, 2019. "Oxidation and alkylation stresses activate ribosome-quality control," Nature Communications, Nature, vol. 10(1), pages 1-15, December.
  • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13579-3
    DOI: 10.1038/s41467-019-13579-3
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-019-13579-3
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-019-13579-3?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. Sammy Villa & Pankaj Dwivedi & Aaron Stahl & Trent Hinkle & Christopher M. Rose & Donald S. Kirkpatrick & Seth M. Tomchik & Vishva M. Dixit & Fred W. Wolf, 2024. "OTUD6 deubiquitination of RPS7/eS7 on the free 40 S ribosome regulates global protein translation and stress," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Joana Silva & Ferhat Alkan & Sofia Ramalho & Goda Snieckute & Stefan Prekovic & Ana Krotenberg Garcia & Santiago Hernández-Pérez & Rob Kammen & Danielle Barnum & Liesbeth Hoekman & Maarten Altelaar & , 2022. "Ribosome impairment regulates intestinal stem cell identity via ZAKɑ activation," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    3. Yoshitaka Matsuo & Takayuki Uchihashi & Toshifumi Inada, 2023. "Decoding of the ubiquitin code for clearance of colliding ribosomes by the RQT complex," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    4. Arun Kumar & Veena Mathew & Peter C. Stirling, 2024. "Dynamics of DNA damage-induced nuclear inclusions are regulated by SUMOylation of Btn2," Nature Communications, Nature, vol. 15(1), pages 1-15, 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:10:y:2019:i:1:d:10.1038_s41467-019-13579-3. 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.