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DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus

Möll, Andrea and Schlimpert, Susan and Briegel, Ariane and Jensen, Grant J. and Thanbichler, Martin (2010) DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus. Molecular Microbiology, 77 (1). pp. 90-107. ISSN 0950-382X. PMCID PMC3057925.

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In bacteria, cytokinesis is dependent on lytic enzymes that facilitate remodelling of the cell wall during constriction. In this work, we identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. It binds to isolated murein sacculi in vitro, and is recruited to the site of constriction through interaction with the cell division protein FtsN. Mutational analyses showed that the LysM domains are necessary and sufficient for localization of DipM, while its peptidase domain is essential for function. Consistent with a role in cell wall hydrolysis, DipM was found to interact with purified murein sacculi in vitro and to induce cell lysis upon overproduction. Its inactivation causes severe defects in outer membrane invagination, resulting in a significant delay between cytoplasmic compartmentalization and final separation of the daughter cells. Overall, these findings indicate that DipM is a periplasmic component of the C. crescentus divisome that facilitates remodelling of the peptidoglycan layer and, thus, coordinated constriction of the cell envelope during the division process.

Item Type:Article
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URLURL TypeDescription CentralArticle
Briegel, Ariane0000-0003-3733-3725
Jensen, Grant J.0000-0003-1556-4864
Thanbichler, Martin0000-0002-1303-1442
Additional Information:© 2010 Blackwell Publishing Ltd. Accepted 15 May, 2010. Published Online: 24 May 2010. We thank Stephanie Wick for excellent technical assistance and Grant R. Bowman, Lucy Shapiro, Yves V. Brun, and Patrick H. Viollier for providing plasmids, strains and antisera. We further thank Sebastian Poggio, Christine Jacobs-Wagner, Erin Goley and Lucy Shapiro for communicating unpublished results. This work was supported by funds from the Max Planck Society, National Institutes of Health (NIH) grant R01 AI067548 to G.J.J., and a gift to Caltech from the Gordon and Betty Moore Foundation.
Funding AgencyGrant Number
Max Planck SocietyUNSPECIFIED
NIHR01 AI067548
Gordon and Betty Moore FoundationUNSPECIFIED
Issue or Number:1
PubMed Central ID:PMC3057925
Record Number:CaltechAUTHORS:20100713-091755026
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:19018
Deposited By: Tony Diaz
Deposited On:28 Jul 2010 15:24
Last Modified:03 Oct 2019 01:51

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