IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v16y2025i1d10.1038_s41467-025-56612-4.html
   My bibliography  Save this article

Structural insights into dynamics of the BMV TLS aminoacylation

Author

Listed:
  • Wen Yang

    (University of Science and Technology of China)

  • Ran Yi

    (University of Science and Technology of China
    Key Laboratory of Anhui Province for Emerging and Reemerging Infectious Diseases)

  • Jing Yao

    (Fudan University
    Fudan University)

  • Yongxiang Gao

    (University of Science and Technology of China)

  • Shanshan Li

    (University of Science and Technology of China
    Key Laboratory of Anhui Province for Emerging and Reemerging Infectious Diseases)

  • Qingguo Gong

    (University of Science and Technology of China)

  • Kaiming Zhang

    (University of Science and Technology of China
    Key Laboratory of Anhui Province for Emerging and Reemerging Infectious Diseases)

Abstract

Brome Mosaic Virus (BMV) utilizes a tRNA-like structure (TLS) within its 3’ untranslated region to mimic host tRNA functions, aiding aminoacylation and viral replication. This study explores the structural dynamics of BMV TLS interacting with tyrosyl-tRNA synthetase (TyrRS) during aminoacylation. Using cryo-EM, we capture multiple states of the TLS-TyrRS complex, including unbound TLS, pre-1a, post-1a, and catalysis states, with resolutions of 4.6 Å, 3.5 Å, 3.7 Å, and 3.85 Å, respectively. These structural comparisons indicate dynamic changes in both TLS and TyrRS. Upon binding, TLS undergoes dynamic rearrangements, particularly with helices B3 and E pivoting, mediated by the unpaired A36 residue, ensuring effective recognition by TyrRS. The dynamic changes also include a more compact arrangement in the catalytic center of TyrRS and the insertion of 3’ CCA end into the enzyme’s active site, facilitating two-steps aminoacylation. Enzymatic assays further demonstrated the functional importance of TLS-TyrRS interactions, with mutations in key residues significantly impacting aminoacylation efficiency. Furthermore, Electrophoretic Mobility Shift Assay (EMSA) demonstrated that BMV TLS binds elongation factors EF1α and EF2, suggesting a multifaceted strategy to exploit host translational machinery. These findings not only enhance our knowledge of virus-host interactions but also offer potential targets for antiviral drug development.

Suggested Citation

  • Wen Yang & Ran Yi & Jing Yao & Yongxiang Gao & Shanshan Li & Qingguo Gong & Kaiming Zhang, 2025. "Structural insights into dynamics of the BMV TLS aminoacylation," Nature Communications, Nature, vol. 16(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-56612-4
    DOI: 10.1038/s41467-025-56612-4
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-025-56612-4
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-025-56612-4?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
    ---><---

    References listed on IDEAS

    as
    1. Muminjon Djumagulov & Natalia Demeshkina & Lasse Jenner & Alexey Rozov & Marat Yusupov & Gulnara Yusupova, 2021. "Accuracy mechanism of eukaryotic ribosome translocation," Nature, Nature, vol. 600(7889), pages 543-546, December.
    2. Timothy M. Colussi & David A. Costantino & John A. Hammond & Grant M. Ruehle & Jay C. Nix & Jeffrey S. Kieft, 2014. "The structural basis of transfer RNA mimicry and conformational plasticity by a viral RNA," Nature, Nature, vol. 511(7509), pages 366-369, July.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Katharina Best & Ken Ikeuchi & Lukas Kater & Daniel Best & Joanna Musial & Yoshitaka Matsuo & Otto Berninghausen & Thomas Becker & Toshifumi Inada & Roland Beckmann, 2023. "Structural basis for clearing of ribosome collisions by the RQT complex," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Yu Shi & Daochao Huang & Cui Song & Ruixue Cao & Zhao Wang & Dan Wang & Li Zhao & Xiaolu Xu & Congyu Lu & Feng Xiong & Haowen Zhao & Shuxiang Li & Quansheng Zhou & Shuyue Luo & Dongjie Hu & Yun Zhang , 2024. "Diphthamide deficiency promotes association of eEF2 with p53 to induce p21 expression and neural crest defects," Nature Communications, Nature, vol. 15(1), pages 1-12, 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:16:y:2025:i:1:d:10.1038_s41467-025-56612-4. 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.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with 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.