Asynchronous division by non-ring FtsZ in the gammaproteobacterial symbiont of Robbea hypermnestra

Leisch, Nikolaus; Pende, N; Weber, Philipp; Gruber‐Vodicka, Harald R.; Verheul, Jolanda; Vischer, Norbert O. E.; Abby, Sophie S.; Geier, Benedikt; Blaauwen, Tanneke den; Bulgheresi, Silvia

doi:10.1038/nmicrobiol.2016.182

Cited by 25 publications

(33 citation statements)

References 36 publications

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“…This organism possesses an operon that encodes for a Min system, but it is not yet clear if Z-ring placement is regulated by the Min system. In another ectosymbiont of same family that also undergoes longitudinal division, it was recently shown that FtsZ accumulation occurs first at a pole proximal to the host (84) (Fig. 6C).…”

Section: Introductionmentioning

confidence: 94%

Bacterial Cell Division: Nonmodels Poised to Take the Spotlight

Eswara

Ramamurthi

2017

Annu. Rev. Microbiol.

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The last three decades have witnessed an explosion in mechanistic details on how model bacterial organisms such as Escherichia coli, Bacillus subtilis, and Caulobacter crescentus undergo binary fission. These advances were possible by not only advances in microscopy that allowed cell biological questions to be answered, but also by the clever use of genetic manipulations in these systems in which specific hypothesis could be directly and easily tested. More recently, research using traditionally understudied organisms, or “non-model” systems, has revealed several alternate mechanistic strategies that bacteria use to divide and propagate. In this review, we will highlight these new findings and compare these strategies to cell division mechanisms elucidated in well-established model organisms.

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Section: Introductionmentioning

confidence: 94%

Bacterial Cell Division: Nonmodels Poised to Take the Spotlight

Eswara

Ramamurthi

2017

Annu. Rev. Microbiol.

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“…Wide field and confocal microscopy of longitudinally dividing symbiotic bacteria that grow while attached with one pole on the skin of marine nematodes can initiate constriction using a discontinuous Z-elipse[72]. In these organisms constriction can also initiate from a single pole, utilizing an arc-like FtsZ structure instead of a ring [73]. Coupled with FtsZ’s strong tendency to form lateral interaction alone in vitro [74], and the large number of proteins identified as “FtsZ bundlers,” (for a review of this class of proteins see [75]) these observations supported a model in which the ring is composed of short FtsZ polymers held together in part via lateral interactions between single stranded protofilaments.…”

Section: Divisome Ultrastructure and The Role Of The “Bundlers”mentioning

confidence: 99%

The divisome at 25: the road ahead

Blaauwen

Hamoen

Levin

2017

Current Opinion in Microbiology

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164

163

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The identification of the FtsZ ring by Bi and Lutkenhaus in 1991 was a defining moment for the field of bacterial cell division. Not only did the presence of the FtsZ ring provide fodder for the next 25 years of research, the application of a then cutting-edge approach-immunogold labeling of bacterial cells-inspired other investigators to apply similarly state-of-the-art technologies in their own work. These efforts have led to important advances in our understanding of the factors underlying assembly and maintenance of the division machinery. At the same time, significant questions about the mechanisms coordinating division with cell growth, DNA replication, and chromosome segregation remain. This review addresses the most prominent of these questions, setting the stage for the next 25 years.

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“…Indeed, mutants of E. coli that constrain active FtsZ to a partial ring structure can still divide, although the cells display abnormal morphologies 11 , 12 . Recent studies have found that many bacterial species naturally initiate constriction on one side of the division site prior to becoming more symmetrical and that these asymmetric constrictions are likely promoted by relatively short FtsZ filaments that do not form a continuous ring structure 13 , 14 .…”

Section: Ftsz the Tubulin Homologmentioning

confidence: 99%

Unite to divide: Oligomerization of tubulin and actin homologs regulates initiation of bacterial cell division

Krupka¹,

Margolin²

2018

F1000Res

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To generate two cells from one, bacteria such as Escherichia coli use a complex of membrane-embedded proteins called the divisome that synthesize the division septum. The initial stage of cytokinesis requires a tubulin homolog, FtsZ, which forms polymers that treadmill around the cell circumference. The attachment of these polymers to the cytoplasmic membrane requires an actin homolog, FtsA, which also forms dynamic polymers that directly bind to FtsZ. Recent evidence indicates that FtsA and FtsZ regulate each other’s oligomeric state in E. coli to control the progression of cytokinesis, including the recruitment of septum synthesis proteins. In this review, we focus on recent advances in our understanding of protein-protein association between FtsZ and FtsA in the initial stages of divisome function, mainly in the well-characterized E. coli system.

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Asynchronous division by non-ring FtsZ in the gammaproteobacterial symbiont of Robbea hypermnestra

Cited by 25 publications

References 36 publications

Bacterial Cell Division: Nonmodels Poised to Take the Spotlight

Bacterial Cell Division: Nonmodels Poised to Take the Spotlight

The divisome at 25: the road ahead

Unite to divide: Oligomerization of tubulin and actin homologs regulates initiation of bacterial cell division

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