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A protein critical for cell constriction in the Gram-negative bacterium Caulobacter crescentus localizes at the division site through its peptidoglycan-binding LysM domains

Lookup NU author(s): Professor Waldemar Vollmer


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P>During division of Gram-negative bacteria, invagination of the cytoplasmic membrane and inward growth of the peptidoglycan (PG) are followed by the cleavage of connective septal PG to allow cell separation. This PG splitting process requires temporal and spatial regulation of cell wall hydrolases. In Escherichia coli, LytM factors play an important role in PG splitting. Here we identify and characterize a member of this family (DipM) in Caulobacter crescentus. Unlike its E. coli counterparts, DipM is essential for viability under fast-growth conditions. Under slow-growth conditions, the Delta dipM mutant displays severe defects in cell division and FtsZ constriction. Consistent with its function in division, DipM colocalizes with the FtsZ ring during the cell cycle. Mutagenesis suggests that the LytM domain of DipM is essential for protein function, despite being non-canonical. DipM also carries two tandems of the PG-binding LysM domain that are sufficient for FtsZ ring localization. Localization and fluorescence recovery after photobleaching microscopy experiments suggest that DipM localization is mediated, at least in part, by the ability of the LysM tandems to distinguish septal, multilayered PG from non-septal, monolayered PG.

Publication metadata

Author(s): Poggio S, Takacs CN, Vollmer W, Jacobs-Wagner C

Publication type: Article

Publication status: Published

Journal: Molecular Microbiology

Year: 2010

Volume: 77

Issue: 1

Pages: 74-89

Print publication date: 24/05/2010

ISSN (print): 0950-382X

ISSN (electronic): 1365-2958

Publisher: Wiley-Blackwell


DOI: 10.1111/j.1365-2958.2010.07223.x


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Funder referenceFunder name
European Commission
Yale College Dean's Office Science, Technology and Research
Howard Hughes Medical Institute
PEW Latin American fellowship
GM076698National Institutes of Health
GM065835National Institutes of Health