Checks and Balances in Bacterial Cell Division

Blaauwen, Tanneke den; Luirink, Joen

doi:10.1128/mbio.00149-19

Cited by 24 publications

(30 citation statements)

References 32 publications

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“…In this regard, it is interesting that cell division in S. aureus was recently reported to be a two‐step process characterized by an initial, slow FtsZ‐dependent activity followed by a faster process when the lipid II flippase, MurJ, arrives and directs peptidoglycan synthesis to the septum (in division stage P2 where SosA expressing cells are stalled) (Monteiro et al , ). More intriguingly, MurJ recruitment in S. aureus was reported to be mediated by the DivIB–FtsL–DivIC complex (Monteiro et al , ), and this complex may serve as a central regulatory hub in bacterial cell division (den Blaauwen and Luirink, ). We hypothesize that this divisional stage could constitute an important molecular cue for the inhibitory activity of SosA, while we keep in mind that the inhibitory activity of SosA could be multifactorial and further studies are required to delineate the exact function of the protein.…”

Section: Discussionmentioning

confidence: 99%

SosA inhibits cell division in Staphylococcus aureus in response to DNA damage

Bojer

Wacnik

Kjelgaard

et al. 2019

Molecular Microbiology

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Summary Inhibition of cell division is critical for viability under DNA‐damaging conditions. DNA damage induces the SOS response that in bacteria inhibits cell division while repairs are being made. In coccoids, such as the human pathogen, Staphylococcus aureus, this process remains poorly studied. Here, we identify SosA as the staphylococcal SOS‐induced cell division inhibitor. Overproduction of SosA inhibits cell division, while sosA inactivation sensitizes cells to genotoxic stress. SosA is a small, predicted membrane protein with an extracellular C‐terminal domain in which point mutation of residues that are conserved in staphylococci and major truncations abolished the inhibitory activity. In contrast, a minor truncation led to SosA accumulation and a strong cell division inhibitory activity, phenotypically similar to expression of wild‐type SosA in a CtpA membrane protease mutant. This suggests that the extracellular C‐terminus of SosA is required both for cell division inhibition and for turnover of the protein. Microscopy analysis revealed that SosA halts cell division and synchronizes the cell population at a point where division proteins such as FtsZ and EzrA are localized at midcell, and the septum formation is initiated but unable to progress to closure. Thus, our findings show that SosA is central in cell division regulation in staphylococci.

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Section: Discussionmentioning

confidence: 99%

SosA inhibits cell division in Staphylococcus aureus in response to DNA damage

Bojer

Wacnik

Kjelgaard

et al. 2019

Molecular Microbiology

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“…The cell division process relies on constriction of the Z-ring that consists of the tubulin homolog FtsZ, a core component of the dynamic divisome complex (3). The Escherichia coli divisome comprises more than twenty different proteins, including SPOR domain protein FtsN and the envelopespanning Tol-Pal complex (4,5). The latter consists of the inner membrane protein TolQ, the inner membrane-anchored periplasmic proteins TolR and TolA, the outer membrane-anchored protein Pal, and the Pal-associated periplasmic protein TolB (5,6).…”

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confidence: 99%

Tol-Pal System and Rgs Proteins Interact to Promote Unipolar Growth and Cell Division in Sinorhizobium meliloti

Krol

Yau

Lechner

et al. 2020

mBio

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Sinorhizobium meliloti is an alphaproteobacterium belonging to the Rhizobiales. Bacteria from this order elongate their cell wall at the new cell pole, generated by cell division. Screening for protein interaction partners of the previously characterized polar growth factors RgsP and RgsM, we identified the inner membrane components of the Tol-Pal system (TolQ and TolR) and novel Rgs (rhizobial growth and septation) proteins with unknown functions. TolQ, Pal, and all Rgs proteins, except for RgsE, were indispensable for S. meliloti cell growth. Six of the Rgs proteins, TolQ, and Pal localized to the growing cell pole in the cell elongation phase and to the septum in predivisional cells, and three Rgs proteins localized to the growing cell pole only. The putative FtsN-like protein RgsS contains a conserved SPOR domain and is indispensable at the early stages of cell division. The components of the Tol-Pal system were required at the late stages of cell division. RgsE, a homolog of the Agrobacterium tumefaciens growth pole ring protein GPR, has an important role in maintaining the normal growth rate and rod cell shape. RgsD is a periplasmic protein with the ability to bind peptidoglycan. Analysis of the phylogenetic distribution of the Rgs proteins showed that they are conserved in Rhizobiales and mostly absent from other alphaproteobacterial orders, suggesting a conserved role of these proteins in polar growth. IMPORTANCE Bacterial cell proliferation involves cell growth and septum formation followed by cell division. For cell growth, bacteria have evolved different complex mechanisms. The most prevalent growth mode of rod-shaped bacteria is cell elongation by incorporating new peptidoglycans in a dispersed manner along the sidewall. A small share of rod-shaped bacteria, including the alphaproteobacterial Rhizobiales, grow unipolarly. Here, we identified and initially characterized a set of Rgs (rhizobial growth and septation) proteins, which are involved in cell division and unipolar growth of Sinorhizobium meliloti and highly conserved in Rhizobiales. Our data expand the knowledge of components of the polarly localized machinery driving cell wall growth and suggest a complex of Rgs proteins with components of the divisome, differing in composition between the polar cell elongation zone and the septum.

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“…FtsZ polymerizes into a structure called the Z ring. The Z ring (i) acts as a scaffold for the recruitment and assembly of several other division proteins, (ii) contributes to the invagination force, and (iii) organizes cell wall remodeling during septation (den Blaauwen & Luirink, 2019). FtsZ does not directly bind to the membrane but depends on adaptor proteins such as FtsA and ZipA.…”

Section: Self‐organization Positioning and Dynamicsmentioning

confidence: 99%

Engineering spatiotemporal organization and dynamics in synthetic cells

Groaz

Moghimianavval

Tavella

et al. 2020

WIREs Nanomed Nanobiotechnol

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Constructing synthetic cells has recently become an appealing area of research. Decades of research in biochemistry and cell biology have amassed detailed part lists of components involved in various cellular processes. Nevertheless, recreating any cellular process in vitro in cell‐sized compartments remains ambitious and challenging. Two broad features or principles are key to the development of synthetic cells—compartmentalization and self‐organization/spatiotemporal dynamics. In this review article, we discuss the current state of the art and research trends in the engineering of synthetic cell membranes, development of internal compartmentalization, reconstitution of self‐organizing dynamics, and integration of activities across scales of space and time. We also identify some research areas that could play a major role in advancing the impact and utility of engineered synthetic cells. This article is categorized under: Biology‐Inspired Nanomaterials > Lipid‐Based Structures Biology‐Inspired Nanomaterials > Protein and Virus‐Based Structures

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Checks and Balances in Bacterial Cell Division

Cited by 24 publications

References 32 publications

SosA inhibits cell division in Staphylococcus aureus in response to DNA damage

SosA inhibits cell division in Staphylococcus aureus in response to DNA damage

Tol-Pal System and Rgs Proteins Interact to Promote Unipolar Growth and Cell Division in Sinorhizobium meliloti

Engineering spatiotemporal organization and dynamics in synthetic cells

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