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

Lookup NU author(s): Dr Jacob BiboyORCiD, Professor Waldemar Vollmer

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

© 2023. The Author(s).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.


Publication metadata

Author(s): Izquierdo-Martinez A, Billini M, Miguel-Ruano V, Hernandez-Tamayo R, Richter P, Biboy J, Batuecas MT, Glatter T, Vollmer W, Graumann PL, Hermoso JA, Thanbichler M

Publication type: Article

Publication status: Published

Journal: Nature Communications

Year: 2023

Volume: 14

Issue: 1

Online publication date: 11/07/2023

Acceptance date: 22/06/2023

Date deposited: 25/07/2023

ISSN (electronic): 2041-1723

Publisher: Springer Nature

URL: https://doi.org/10.1038/s41467-023-39783-w

DOI: 10.1038/s41467-023-39783-w

PubMed id: 37433794


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Funding

Funder referenceFunder name
EP/T002778/1EPSRC
CRSII5_198737/1
German Research Foundation
Max Planck Society
PID2020-115331GB-I00
University of Marburg

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