Interaction of the Morphogenic Protein RodZ with the Bacillus subtilis Min System

Muchová, Katarı́na; Chromiková, Zuzana; Valenčíková, Romana; Barák, Imrich

doi:10.3389/fmicb.2017.02650

Cited by 6 publications

(12 citation statements)

References 41 publications

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“…How MinD, a protein in the cytoplasm, would inhibit peptidoglycan extracellular remodeling is unclear, but we note the B. subtilis Min system interacts with a polarly localized multipass transmembrane protein, MinJ (43,44). MinJ has recently been shown to interact with RodZ, a protein involved in peptidoglycan synthesis/remodeling, and perhaps the MinCDJ complex keeps RodZ away from the poles (88)(89)(90)(91). Moreover, why minicells fail to grow is poorly understood, but perhaps it is due to the fact that they quickly lose the ability to remodel their peptidoglycan.…”

Section: Discussionmentioning

confidence: 98%

The Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in Bacillus subtilis

Zhou

Dempwolff

et al. 2020

mBio

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A microfluidic system coupled with fluorescence microscopy is a powerful approach for quantitative analysis of bacterial growth. Here, we measure parameters of growth and dynamic localization of the cell division initiation protein FtsZ in Bacillus subtilis. Consistent with previous reports, we found that after division, FtsZ rings remain at the cell poles, and polar FtsZ ring disassembly coincides with rapid Z-ring accumulation at the midcell. In cells mutated for minD, however, the polar FtsZ rings persist indefinitely, suggesting that the primary function of the Min system is in Z-ring disassembly. The inability to recycle FtsZ monomers in the minD mutant results in the simultaneous maintenance of multiple Z-rings that are restricted by competition for newly synthesized FtsZ. Although the parameters of FtsZ dynamics change in the minD mutant, the overall cell division time remains the same, albeit with elongated cells necessary to accumulate a critical threshold amount of FtsZ for promoting medial division. Finally, the minD mutant characteristically produces minicells composed of polar peptidoglycan shown to be inert for remodeling in the wild type. Polar peptidoglycan, however, loses its inert character in the minD mutant, suggesting that the Min system not only is important for recycling FtsZ but also may have a secondary role in the spatiotemporal regulation of peptidoglycan remodeling. IMPORTANCE Many bacteria grow and divide by binary fission in which a mother cell divides into two identical daughter cells. To produce two equally sized daughters, the division machinery, guided by FtsZ, must dynamically localize to the midcell each cell cycle. Here, we quantitatively analyzed FtsZ dynamics during growth and found that the Min system of Bacillus subtilis is essential to disassemble FtsZ rings after division. Moreover, a failure to efficiently recycle FtsZ results in an increase in cell size. Finally, we show that the Min system has an additional role in inhibiting cell wall turnover and contributes to the “inert” property of cell walls at the poles.

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Section: Discussionmentioning

confidence: 98%

The Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in Bacillus subtilis

Zhou

Dempwolff

et al. 2020

mBio

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“…How MinD, a protein in the cytoplasm would inhibit peptidoglycan remodeling extracellularly is unclear, but we note the B. subtilis Min system interacts with a polarly-localized multi-pass transmembrane protein, MinJ (43, 44). MinJ has recently been shown to interact with RodZ, a protein involved in peptidoglycan synthesis/remodeling, and perhaps the MinCDJ complex keeps RodZ away from the poles (84–87). Moreover, why mincells fail to grow is poorly understood, but perhaps, they quickly lose the ability to remodel their peptidoglycan.…”

Section: Discussionmentioning

confidence: 99%

The Min system disassembles FtsZ foci and inhibits polar peptidoglycan remodeling inBacillus subtilis

Zhou

Dempwollf

et al. 2019

Preprint

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lack DNA and arise when cell division occurs, not at the midcell, but rather near one cell pole. 75Polar division was attributed to a mislocalization of FtsZ rings and the recruitment of the same 76 machinery that would ordinarily promote medial septation (20). The mutation responsible for 77 minicell formation was mapped to a genetic locus encoding the membrane-associated ATPase 78MinD and the 22). MinD is anchored to the membrane by an 79 amphipathic helix, and MinD recruits and activates MinC by direct interaction (23-30). MinC 80 binds to the C-terminus of FtsZ and destabilizes the FtsZ ring (31)(32)(33)(34)(35). In E. coli, the activity of 81 the MinCD complex is dynamically restricted to the polar region by oscillation in which MinCD 82 polar polymerization is antagonized by MinE-mediated depolymerization (36-40). In B. subtilis 83 however, the activity of the MinCD complex is statically restricted to membranes with high 84 curvature by MinJ/DivIVA, such that the entire 4-protein complex assembles at the invaginating 85 nascent division plane and remains at the cell poles after division (41)(42)(43)(44)(45)(46). 86Here, we use fluorescence microscopy and microfluidics to quantitatively measure 87 parameters of B. subtilis FtsZ dynamics and cell division under the condition of chemostatic 88 growth for extended periods of time (47-52). The automated poly(dimethylsiloxane) microfluidic 89 system comprises a pneumatically actuated channel array of 600 channels having widths from 90 1.0 to 1.6 m and heights of 1.0 m to actively trap bacteria cells (52). Integrated pumps and 91 valves perform on-chip fluid and cell manipulations that provide dynamic control of cell loading 92 and nutrient flow, and the channel array confines bacterial growth to a single dimension, 93 facilitating high-resolution, time-lapse imaging and tracking of individual cells over multiple 94 generations. In wild type cells, we find that Z-rings persist for a period greater than one cell 95 cycle because Z-rings transiently remain at the cell poles following septum completion. We 96 further show find that the primary function of the Min system is Z-ring disassembly such that in 97 the absence of Min, Z-rings persist longer than the duration of the experiment. Indefinite Z-ring 98 persistence results in cells with multiple Z-rings per compartment, and Z-ring must directly 99 compete for newly synthesized FtsZ monomers. Moreover, we show that min mutant cells are 100

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“…The second strain with an instable diameter is Δ minJ . This mutant of the “Min” system, a complex in charge of controlling the placement of the divisome, is known to present a reduced septum formation leading to long cells ( 61, 65 ). Although its average cell width was marginally affected (-1%), the standard deviation was unusually large, and extreme widths ranged from 0.6 to 1.5 µm (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Sup. 5B), indicative of the perturbation of the division process ( 65 ). When grown on the slightly poorer MSM, a casamino-acids-based medium, phenotypes of rodZ mutant cells worsen: cells widen, frequently divided asymmetrically (Fig.…”

Section: Resultsmentioning

confidence: 99%

A high content microscopy screening identifies new genes involved in cell width control inBacillus subtilis

Juillot

Cornilleau

Deboosère

et al. 2021

Preprint

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How cells control their size is a fundamental question of biology. In bacteria, cell shape is imposed by the extracellular cell wall, in particular by the continuous polymer of peptidoglycan (PG) that surrounds the cell. Thus, bacterial cell morphogenesis results from the coordinated action of the proteins assembling and degrading the PG shell. Remarkably, during steady-state growth, most bacteria maintain a defined shape along generations, suggesting that an error-proof mechanism tightly controls the process. In the rod-shaped model for Gram-positive bacteria, Bacillus subtilis, it is well known that the average cell length varies as a function of growth rate but that cell diameter remains constant throughout its cell cycle and across growth conditions. Here, in an attempt to shed light on the cellular circuits controlling bacterial cell width, we developed a screen to identify genetic determinants of cell width in B. subtilis. Using HCS (high-content screening) fluorescence microscopy and semi-automated measurement of single-cell dimensions, we screened a library of ~ 4000 single knockout mutants. We identified 12 mutations significantly altering cell diameter, in genes that belong to several functional groups. In particular, these results highlight a link between cell width control and metabolism.

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Interaction of the Morphogenic Protein RodZ with the Bacillus subtilis Min System

Cited by 6 publications

References 41 publications

The Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in Bacillus subtilis

The Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in Bacillus subtilis

The Min system disassembles FtsZ foci and inhibits polar peptidoglycan remodeling inBacillus subtilis

A high content microscopy screening identifies new genes involved in cell width control inBacillus subtilis

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