Rapid pole-to-pole oscillation of a protein required for directing division to the middle of
            <i>Escherichia coli</i>

Raskin, David M.; Boer, Piet A. J. de

doi:10.1073/pnas.96.9.4971

Cited by 694 publications

(912 citation statements)

References 26 publications

(38 reference statements)

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“…One important inhibitory system, the MIN SYSTEM, is crucial for the precise positioning of the Z ring. In E. coli, this system consists of the FtsZ assembly inhibitor MinC, and the MinD and MinE proteins, which oscillate from one cell pole to the other 40,41 . MinD is an ATPase that binds to the membrane in its ATP form and is released from the membrane on ATP hydrolysis.…”

Section: Regulation Of Z-ring Assembly Spatial Regulationmentioning

confidence: 99%

FtsZ and the division of prokaryotic cells and organelles

Margolin

2005

Nat Rev Mol Cell Biol

558

484

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Binary fission of many prokaryotes as well as some eukaryotic organelles depends on the FtsZ protein, which self-assembles into a membrane-associated ring structure early in the division process. FtsZ is homologous to tubulin, the building block of the microtubule cytoskeleton in eukaryotes. Recent advances in genomics and cell-imaging techniques have paved the way for the remarkable progress in our understanding of fission in bacteria and organelles.Duplication of cells occurs by the division of a mother cell into two daughter cells. This process, known as cytokinesis, provides the force to split cells and is spatially regulated to faithfully partition the genetic material. The cytoskeleton has a crucial role in cytokinesis. In animal and fungal cells, a medial ring of actin and myosin, helped by other proteins, contracts to divide the cell. Plant cells use a cell plate, and are guided by actin filaments and microtubules. Prokaryotes, which include bacteria and archaea, possess homologues of eukaryotic cytoskeletal proteins. Most prokaryotes use a tubulin homologue, a protein known as FtsZ, to divide. Eukaryotic organelles such as chloroplasts and mitochondria evolved from bacteria, and all chloroplasts and some mitochondria use FtsZ to divide.FtsZ is thought to be the first protein to localize to the site of future division in bacteria 1 , and it assembles into what is known as the Z ring (FIG. 1). In Escherichia coli, the Z ring recruits at least ten other proteins, all of which are required for the progression and completion of cytokinesis 2 , as will be discussed below. Whereas the cytokinetic apparatus in eukaryotic cells and even organelles can be observed directly in stained thin sections by transmission electron microscopy, the Z ring and its associated factors are not detectable by these methods. This is probably because the protein machinery is largely membrane bound and resides in a densely populated cytoplasmic environment. However, the development of green fluorescent protein (GFP) fusion and improved immunofluorescence techniques over the past 10 years have been crucial in allowing the first direct visualization of many cellular components and their dynamics. For example, using GFP fusions, the dynamics of the Z ring and other components of the cell-division protein machinery can now be visualized in living bacterial cells. The combination of these new cytological tools with genomics and the Competing interests statementThe author declares no competing financial interests. HHS Public Access Author Manuscript Author ManuscriptAuthor ManuscriptAuthor Manuscript already powerful genetics of several model systems have spurred rapid progress in our understanding of the molecular cell biology of bacteria and eukaryotic organelles. This review will discuss how the recent revolutions in genomics and cell biology have provided new evolutionary and mechanistic insights into how bacterial cells and organelles divide. The FtsZ family of proteins Conservation of FtsZFtsZ is a highly conserved protein ...

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Section: Regulation Of Z-ring Assembly Spatial Regulationmentioning

confidence: 99%

FtsZ and the division of prokaryotic cells and organelles

Margolin

2005

Nat Rev Mol Cell Biol

558

484

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“…A striking example of protein self‐organization is the Min protein system (comprising the proteins MinC, MinD, and MinE) of the bacterium Escherichia coli ,1 which oscillates between the cell poles. These pole‐to‐pole oscillations generate a time‐averaged non‐homogeneous concentration gradient with a minimum at the mid‐cell plane, the future cell division site 2, 3, 4, 5, 6, 7. Intriguingly, only a minimal set of components (the two membrane interacting proteins MinD and MinE, a lipid membrane, and ATP) has been shown to establish Min oscillations 8, 9, 10, 11, 12.…”

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confidence: 99%

Protein Patterns and Oscillations on Lipid Monolayers and in Microdroplets

2016

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The Min proteins from E.coli position the bacterial cell‐division machinery through pole‐to‐pole oscillations. In vitro, Min protein self‐organization can be reconstituted in the presence of a lipid membrane as a catalytic surface. However, Min dynamics have so far not been reconstituted in fully membrane‐enclosed volumes. Microdroplets interfaced by lipid monolayers were employed as a simple 3D mimic of cellular compartments to reconstitute Min protein oscillations. We demonstrate that lipid monolayers are sufficient to fulfil the catalytic role of the membrane and thus represent a facile platform to investigate Min protein regulated dynamics of the cell‐division protein FtsZ‐mts. In particular, we show that droplet containers reveal distinct Min oscillation modes, and reveal a dependence of FtsZ‐mts structures on compartment size. Finally, co‐reconstitution of Min proteins and FtsZ‐mts in droplets yields antagonistic localization, thus demonstrating that droplets indeed support the analysis of complex bacterial self‐organization in confined volumes.

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“…13 As can be seen, the MinD concentration is nicely minimized at the cell center for shorter cell lengths. However, as the cell length increases, the precision with which the center can be identified is considerably reduced, with the averaged signal fluctuating considerably at 8 mm.…”

Section: Results: Polar Protein Localizationmentioning

confidence: 64%

A Mechanism for Polar Protein Localization in Bacteria

Howard

2004

Journal of Molecular Biology

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We investigate a mechanism for the polar localization of proteins in bacteria. We focus on the MinCD/DivIVA system regulating division site placement in the rod-shaped bacterium Bacillus subtilis. Our model relies on a combination of geometric effects and reaction-diffusion dynamics to direct proteins to both cell poles, where division is then blocked. We discuss similarities and differences with related division models in Escherichia coli and also develop extensions of the model to asymmetric polar protein localization. We propose that our mechanism for polar localization may be employed more widely in bacteria, especially in outgrowing spores, which do not possess any pre-existing polar division apparatus from prior division events.

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Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli

Cited by 694 publications

References 26 publications

FtsZ and the division of prokaryotic cells and organelles

FtsZ and the division of prokaryotic cells and organelles

Protein Patterns and Oscillations on Lipid Monolayers and in Microdroplets

A Mechanism for Polar Protein Localization in Bacteria

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