IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v14y2023i1d10.1038_s41467-023-39783-w.html
   My bibliography  Save this article

DipM controls multiple autolysins and mediates a regulatory feedback loop promoting cell constriction in Caulobacter crescentus

Author

Listed:
  • Adrian Izquierdo-Martinez

    (University of Marburg
    Max Planck Institute for Terrestrial Microbiology
    Universidade Nova de Lisboa)

  • Maria Billini

    (University of Marburg)

  • Vega Miguel-Ruano

    (Instituto de Química-Física “Rocasolano”, Consejo Superior de Investigaciones Científicas)

  • Rogelio Hernández-Tamayo

    (University of Marburg
    Center for Synthetic Microbiology (SYNMIKRO))

  • Pia Richter

    (University of Marburg)

  • Jacob Biboy

    (Newcastle University)

  • María T. Batuecas

    (Instituto de Química-Física “Rocasolano”, Consejo Superior de Investigaciones Científicas)

  • Timo Glatter

    (Max Planck Institute for Terrestrial Microbiology)

  • Waldemar Vollmer

    (Newcastle University
    The University of Queensland)

  • Peter L. Graumann

    (University of Marburg
    Center for Synthetic Microbiology (SYNMIKRO))

  • Juan A. Hermoso

    (Instituto de Química-Física “Rocasolano”, Consejo Superior de Investigaciones Científicas)

  • Martin Thanbichler

    (University of Marburg
    Max Planck Institute for Terrestrial Microbiology
    Center for Synthetic Microbiology (SYNMIKRO))

Abstract

Proteins with a catalytically inactive LytM-type endopeptidase domain are important regulators of cell wall-degrading enzymes in bacteria. Here, we study their representative DipM, a factor promoting cell division in Caulobacter crescentus. We show that the LytM domain of DipM interacts with multiple autolysins, including the soluble lytic transglycosylases SdpA and SdpB, the amidase AmiC and the putative carboxypeptidase CrbA, and stimulates the activities of SdpA and AmiC. Its crystal structure reveals a conserved groove, which is predicted to represent the docking site for autolysins by modeling studies. Mutations in this groove indeed abolish the function of DipM in vivo and its interaction with AmiC and SdpA in vitro. Notably, DipM and its targets SdpA and SdpB stimulate each other’s recruitment to midcell, establishing a self-reinforcing cycle that gradually increases autolytic activity as cytokinesis progresses. DipM thus coordinates different peptidoglycan-remodeling pathways to ensure proper cell constriction and daughter cell separation.

Suggested Citation

  • Adrian Izquierdo-Martinez & Maria Billini & Vega Miguel-Ruano & Rogelio Hernández-Tamayo & Pia Richter & Jacob Biboy & María T. Batuecas & Timo Glatter & Waldemar Vollmer & Peter L. Graumann & Juan A., 2023. "DipM controls multiple autolysins and mediates a regulatory feedback loop promoting cell constriction in Caulobacter crescentus," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
  • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-39783-w
    DOI: 10.1038/s41467-023-39783-w
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-023-39783-w
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-023-39783-w?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. Sergio G. Bartual & Daniel Straume & Gro Anita Stamsås & Inés G. Muñoz & Carlos Alfonso & Martín Martínez-Ripoll & Leiv Sigve Håvarstein & Juan A. Hermoso, 2014. "Structural basis of PcsB-mediated cell separation in Streptococcus pneumoniae," Nature Communications, Nature, vol. 5(1), pages 1-12, September.
    2. Martín Alcorlo & David A. Dik & Stefania Benedetti & Kiran V. Mahasenan & Mijoon Lee & Teresa Domínguez-Gil & Dusan Hesek & Elena Lastochkin & Daniel López & Bill Boggess & Shahriar Mobashery & Juan A, 2019. "Structural basis of denuded glycan recognition by SPOR domains in bacterial cell division," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    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. Jianwei Li & Xin Xu & Jian Shi & Juan A. Hermoso & Lok-To Sham & Min Luo, 2023. "Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    2. Zhixin Lyu & Atsushi Yahashiri & Xinxing Yang & Joshua W. McCausland & Gabriela M. Kaus & Ryan McQuillen & David S. Weiss & Jie Xiao, 2022. "FtsN maintains active septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthases in E. coli," Nature Communications, Nature, vol. 13(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:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-39783-w. 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.