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

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. Hermoso and Martin Thanbichler ()
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Adrian Izquierdo-Martinez: University of Marburg
Maria Billini: University of Marburg
Vega Miguel-Ruano: Instituto de Química-Física “Rocasolano”, Consejo Superior de Investigaciones Científicas
Rogelio Hernández-Tamayo: University of Marburg
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
Peter L. Graumann: University of Marburg
Juan A. Hermoso: Instituto de Química-Física “Rocasolano”, Consejo Superior de Investigaciones Científicas
Martin Thanbichler: University of Marburg

Nature Communications, 2023, vol. 14, issue 1, 1-18

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-39783-w

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