IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-35607-5.html
   My bibliography  Save this article

Peptidoglycan recycling mediated by an ABC transporter in the plant pathogen Agrobacterium tumefaciens

Author

Listed:
  • Michael C. Gilmore

    (Umeå University)

  • Felipe Cava

    (Umeå University)

Abstract

During growth and division, the bacterial cell wall peptidoglycan (PG) is remodelled, resulting in the liberation of PG muropeptides which are typically reinternalized and recycled. Bacteria belonging to the Rhizobiales and Rhodobacterales orders of the Alphaproteobacteria lack the muropeptide transporter AmpG, despite having other key PG recycling enzymes. Here, we show that an alternative transporter, YejBEF-YepA, takes over this role in the Rhizobiales phytopathogen Agrobacterium tumefaciens. Muropeptide import by YejBEF-YepA governs expression of the β-lactamase AmpC in A. tumefaciens, contributing to β-lactam resistance. However, we show that the absence of YejBEF-YepA causes severe cell wall defects that go far beyond lowered AmpC activity. Thus, contrary to previously established Gram-negative models, PG recycling is vital for cell wall integrity in A. tumefaciens. YepA is widespread in the Rhizobiales and Rhodobacterales, suggesting that YejBEF-YepA-mediated PG recycling could represent an important but overlooked aspect of cell wall biology in these bacteria.

Suggested Citation

  • Michael C. Gilmore & Felipe Cava, 2022. "Peptidoglycan recycling mediated by an ABC transporter in the plant pathogen Agrobacterium tumefaciens," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-35607-5
    DOI: 10.1038/s41467-022-35607-5
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-35607-5
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-022-35607-5?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. Paulina Seweryn & Lan Bich Van & Morten Kjeldgaard & Christopher J. Russo & Lori A. Passmore & Bjarne Hove-Jensen & Bjarne Jochimsen & Ditlev E. Brodersen, 2015. "Structural insights into the bacterial carbon–phosphorus lyase machinery," Nature, Nature, vol. 525(7567), pages 68-72, September.
    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. Søren K. Amstrup & Sui Ching Ong & Nicholas Sofos & Jesper L. Karlsen & Ragnhild B. Skjerning & Thomas Boesen & Jan J. Enghild & Bjarne Hove-Jensen & Ditlev E. Brodersen, 2023. "Structural remodelling of the carbon–phosphorus lyase machinery by a dual ABC ATPase," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Dingyi Wang & Mingjie Li & Chengdong Shuang & Yong Liang & Yue Zhao & Minyan Wang & Zhuangzhi Shi, 2022. "Rhodium-catalyzed selective direct arylation of phosphines with aryl bromides," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    3. Leandro Israel da Silva & Marlon Correa Pereira & André Mundstock Xavier de Carvalho & Victor Hugo Buttrós & Moacir Pasqual & Joyce Dória, 2023. "Phosphorus-Solubilizing Microorganisms: A Key to Sustainable Agriculture," Agriculture, MDPI, vol. 13(2), pages 1-30, February.

    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:13:y:2022:i:1:d:10.1038_s41467-022-35607-5. 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.