IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v500y2013i7462d10.1038_nature12453.html
   My bibliography  Save this article

PAAR-repeat proteins sharpen and diversify the type VI secretion system spike

Author

Listed:
  • Mikhail M. Shneider

    (École Polytechnique Fédérale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland
    Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Laboratory of Molecular Bioengineering, 16/10 Miklukho-Maklaya Street, 117997 Moscow, Russia)

  • Sergey A. Buth

    (École Polytechnique Fédérale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland)

  • Brian T. Ho

    (Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA)

  • Marek Basler

    (Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA)

  • John J. Mekalanos

    (Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA)

  • Petr G. Leiman

    (École Polytechnique Fédérale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland)

Abstract

An X-ray structure of bacterial type VI secretion system components reveals that PAAR family proteins bind at the tip of the VgrG spike, providing new insights into the mechanisms of type VI secretion; experiments using bacteria confirmed the importance of PAAR proteins.

Suggested Citation

  • Mikhail M. Shneider & Sergey A. Buth & Brian T. Ho & Marek Basler & John J. Mekalanos & Petr G. Leiman, 2013. "PAAR-repeat proteins sharpen and diversify the type VI secretion system spike," Nature, Nature, vol. 500(7462), pages 350-353, August.
  • Handle: RePEc:nat:nature:v:500:y:2013:i:7462:d:10.1038_nature12453
    DOI: 10.1038/nature12453
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature12453
    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/nature12453?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. Katarzyna Kanarek & Chaya Mushka Fridman & Eran Bosis & Dor Salomon, 2023. "The RIX domain defines a class of polymorphic T6SS effectors and secreted adaptors," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Dukas Jurėnas & Leonardo Talachia Rosa & Martial Rey & Julia Chamot-Rooke & Rémi Fronzes & Eric Cascales, 2021. "Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    3. Xiaoying Cai & Yao He & Iris Yu & Anthony Imani & Dean Scholl & Jeff F. Miller & Z. Hong Zhou, 2024. "Atomic structures of a bacteriocin targeting Gram-positive bacteria," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    4. Thibault R. Bongiovanni & Casey J. Latario & Youn Cras & Evan Trus & Sophie Robitaille & Kerry Swartz & Danica Schmidtke & Maxence Vincent & Artemis Kosta & Jan Orth & Florian Stengel & Riccardo Pella, 2024. "Assembly of a unique membrane complex in type VI secretion systems of Bacteroidota," Nature Communications, Nature, vol. 15(1), pages 1-16, 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:500:y:2013:i:7462:d:10.1038_nature12453. 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.