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Bacterial physiology: Life minus Z

Nature Microbiology volume 1, Article number: 16121 (2016) Cite this article

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The surprising discovery of viable mutants that retain a peptidoglycan cell wall but lack the essential director of normal cytokinesis, FtsZ, reveals that Escherichia coli can proliferate in a completely unexpected manner.

FtsZ is an ancient protein that directs cytokinesis in almost all Bacteria and Euryarchaeota, as well as plastidial and mitochondrial fission in many eukaryotic species3,4. In preparation for cell fission, homopolymers of FtsZ accumulate at the future division site (usually midcell) together with protein partners that tether them to the cytoplasmic membrane. This Z-ring then recruits additional division proteins to form a mature septal ring organelle or divisome, which subsequently drives the coordinated invagination of the cell envelope layers and sister cell separation. Integral to the septal ring are specialized PG enzymes that have the onerous tasks of producing an inward growing annulus of septal peptidoglycan that remains continuous with the cylindrical portion of the mother sacculus, and then to cautiously split this layer from the outside inwards to generate the two new hemispherical caps of the nascent sister sacculi. When FtsZ function becomes compromised, the septal ring cannot form and cells fail to divide. Other cell cycle events are not immediately affected, however, and FtsZ-depleted cells of rod-shaped organisms typically elongate into long multiploid filamentous cells before eventually dying (Fig. 1c)1,3.

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Figure 1: Plasticity in E. coli cell shape and proliferation.

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  1. Piet A. J. de Boer is in the Department of Molecular Biology & Microbiology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4960, USA.,

    Piet A. J. de Boer

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Correspondence to Piet A. J. de Boer.

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de Boer, P. Bacterial physiology: Life minus Z. Nat Microbiol 1, 16121 (2016). https://doi.org/10.1038/nmicrobiol.2016.121

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