Bacterial Cell Division: Nonmodels Poised to Take the Spotlight

Eswara, Prahathees J.; Ramamurthi, Kumaran S.

doi:10.1146/annurev-micro-102215-095657

Cited by 78 publications

(68 citation statements)

References 146 publications

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“…The Min reaction network has been extensively studied in various organisms [8, 81]. In E. coli , it was found to be a highly dynamic and self-organizing system capable of pole-to-pole oscillation, a prime example for intracellular protein pattern formation [34].…”

Section: Discussionmentioning

confidence: 99%

Dynamics of theBacillus subtilisMin system

Feddersen

Wuerthner

Frey

et al. 2020

Preprint

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SummaryDivision site selection is a vital process to ensure generation of viable offspring. In many rod-shaped bacteria a dynamic protein system, termed the Min system, acts as a central regulator of division site placement. The Min system is best studied in Escherichia coli where it shows a remarkable oscillation from pole to pole with a time-averaged density minimum at midcell. Several components of the Min system are conserved in the Gram-positive model organism Bacillus subtilis. However, in B. subtilis it is believed that the system forms a stationary bipolar gradient from the cell poles to midcell. Here, we show that the Min system of B. subtilis localizes dynamically to active sites of division, often organized in clusters. We provide physical modelling using measured diffusion constants that describe the observed enrichment of the Min system at the septum. Modelling suggests that the observed localization pattern of Min proteins corresponds to a dynamic equilibrium state. Our data provide evidence for the importance of ongoing septation for the Min dynamics, consistent with a major role of the Min system to control active division sites, but not cell pole areas.

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Section: Discussionmentioning

confidence: 99%

Dynamics of theBacillus subtilisMin system

Feddersen

Wuerthner

Frey

et al. 2020

Preprint

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“…The question of how the division site is defined is central also in bacterial division. In E. coli , the best-studied model, two negative regulatory mechanisms have been described, based on nucleoid occlusion or on the Min system 61 . No orthologs for either of these systems have been detected in mitochondria 10 , where the nucleoid has been suggested to act as a spatial organizer of the mitochondrial fission machinery.…”

Section: Discussionmentioning

confidence: 99%

Bacterial FtsZ induces mitochondrial fission in human cells

Spier

Sachse

Tham

et al. 2020

Preprint

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32Mitochondria are key eukaryotic organelles that evolved from an intracellular bacterium, 33 in a process involving bacterial genome rearrangement and streamlining. As 34 mitochondria cannot form de novo, their biogenesis relies on growth and division. In 35 human cells, mitochondrial division plays an important role in processes as diverse as 36 mtDNA distribution, mitochondrial transport and quality control. Consequently, defects 37 in mitochondrial division have been associated with a wide range of human pathologies. 38While several protists have retained key components of the bacterial division machinery, 39 none have been detected in human mitochondria, where the dynamin-related protein 40 Drp1, a cytosolic GTPase is recruited to the mitochondrial outer membrane, forming 41 helical oligomers that constrict and divide mitochondria. Here, we created a human codon 42 optimized version of FtsZ, the central component of the bacterial division machinery, and 43 fused it to a mitochondrial targeting sequence. Upon expression in human cells, mt-FtsZ 44 was imported into the mitochondrial matrix, specifically localizing at fission sites prior to 45Drp1 and significantly increasing mitochondrial fission levels. Our data suggests that 46 human mitochondria have an internal, matrix-localized fission machinery, whose 47 structure is sufficiently conserved as to accommodate bacterial FtsZ. We identified 48 interaction partners of mt-FtsZ, and show that expression of PGAM5, FAM210, SFXN3 and 49 MTCH1 induced mitochondrial fission. Our results thus represent an innovative approach 50 for the discovery of novel critical mitochondrial fission components. 51 52 53

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“…The partner to this resilience is fastidiousness. Bacterium grow and divide with consummate orchestration . As its genome is replicated within its cytoplasm the structural entities of its cell envelope—lipids, proteins, glycans, and a peptidoglycan cell‐wall polymer—are synthesized and assembled .…”

Section: Introductionmentioning

confidence: 99%

“…Bacterium grow and divide with consummate orchestration. [1][2][3] As its genome is replicated within its cytoplasm 4,5 the structural entities of its cell envelope-lipids, proteins, glycans, and a peptidoglycan cell-wall polymer-are synthesized and assembled. 6 Minutes later the daughter cells separate by the fracturing of their shared septal cell envelope.…”

Section: Introductionmentioning

confidence: 99%

Constructing and deconstructing the bacterial cell wall

Fisher

Mobashery

2019

Protein Science

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The history of modern medicine cannot be written apart from the history of the antibiotics. Antibiotics are cytotoxic secondary metabolites that are isolated from Nature. The antibacterial antibiotics disproportionately target bacterial protein structure that is distinct from eukaryotic protein structure, notably within the ribosome and within the pathways for bacterial cell‐wall biosynthesis (for which there is not a eukaryotic counterpart). This review focuses on a pre‐eminent class of antibiotics—the β‐lactams, exemplified by the penicillins and cephalosporins—from the perspective of the evolving mechanisms for bacterial resistance. The mechanism of action of the β‐lactams is bacterial cell‐wall destruction. In the monoderm (single membrane, Gram‐positive staining) pathogen Staphylococcus aureus the dominant resistance mechanism is expression of a β‐lactam‐unreactive transpeptidase enzyme that functions in cell‐wall construction. In the diderm (dual membrane, Gram‐negative staining) pathogen Pseudomonas aeruginosa a dominant resistance mechanism (among several) is expression of a hydrolytic enzyme that destroys the critical β‐lactam ring of the antibiotic. The key sensing mechanism used by P. aeruginosa is monitoring the molecular difference between cell‐wall construction and cell‐wall deconstruction. In both bacteria, the resistance pathways are manifested only when the bacteria detect the presence of β‐lactams. This review summarizes how the β‐lactams are sensed and how the resistance mechanisms are manifested, with the expectation that preventing these processes will be critical to future chemotherapeutic control of multidrug resistant bacteria.

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Bacterial Cell Division: Nonmodels Poised to Take the Spotlight

Cited by 78 publications

References 146 publications

Dynamics of theBacillus subtilisMin system

Dynamics of theBacillus subtilisMin system

Bacterial FtsZ induces mitochondrial fission in human cells

Constructing and deconstructing the bacterial cell wall

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