IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v9y2018i1d10.1038_s41467-018-04305-6.html
   My bibliography  Save this article

Hierarchical mechanism of amino acid sensing by the T-box riboswitch

Author

Listed:
  • Krishna C. Suddala

    (University of Michigan
    University of Michigan)

  • Javier Cabello-Villegas

    (University of Michigan)

  • Malgorzata Michnicka

    (Rice University)

  • Collin Marshall

    (University of Michigan)

  • Edward P. Nikonowicz

    (Rice University)

  • Nils G. Walter

    (University of Michigan)

Abstract

In Gram-positive bacteria, T-box riboswitches control gene expression to maintain the cellular pools of aminoacylated tRNAs essential for protein biosynthesis. Co-transcriptional binding of an uncharged tRNA to the riboswitch stabilizes an antiterminator, allowing transcription read-through, whereas an aminoacylated tRNA does not. Recent structural studies have resolved two contact points between tRNA and Stem-I in the 5′ half of the T-box riboswitch, but little is known about the mechanism empowering transcriptional control by a small, distal aminoacyl modification. Using single-molecule fluorescence microscopy, we have probed the kinetic and structural underpinnings of tRNA binding to a glycyl T-box riboswitch. We observe a two-step mechanism where fast, dynamic recruitment of tRNA by Stem-I is followed by ultra-stable anchoring by the downstream antiterminator, but only without aminoacylation. Our results support a hierarchical sensing mechanism wherein dynamic global binding of the tRNA body is followed by localized readout of its aminoacylation status by snap-lock-based trapping.

Suggested Citation

  • Krishna C. Suddala & Javier Cabello-Villegas & Malgorzata Michnicka & Collin Marshall & Edward P. Nikonowicz & Nils G. Walter, 2018. "Hierarchical mechanism of amino acid sensing by the T-box riboswitch," Nature Communications, Nature, vol. 9(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04305-6
    DOI: 10.1038/s41467-018-04305-6
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-018-04305-6
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-018-04305-6?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. Krishna C. Suddala & Janghyun Yoo & Lixin Fan & Xiaobing Zuo & Yun-Xing Wang & Hoi Sung Chung & Jinwei Zhang, 2023. "Direct observation of tRNA-chaperoned folding of a dynamic mRNA ensemble," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Adrien Chauvier & Shiba S. Dandpat & Rosa Romero & Nils G. Walter, 2024. "A nascent riboswitch helix orchestrates robust transcriptional regulation through signal integration," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    3. Eduardo Campos-Chavez & Sneha Paul & Zunwu Zhou & Dulce Alonso & Anjali R. Verma & Jingyi Fei & Alfonso Mondragón, 2024. "Translational T-box riboswitches bind tRNA by modulating conformational flexibility," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    4. Xiaolin Niu & Zhonghe Xu & Yufan Zhang & Xiaobing Zuo & Chunlai Chen & Xianyang Fang, 2023. "Structural and dynamic mechanisms for coupled folding and tRNA recognition of a translational T-box riboswitch," Nature Communications, Nature, vol. 14(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:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04305-6. 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.