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

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  • 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
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    References listed on IDEAS

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    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.
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