MinDE-Dependent Pole-to-Pole Oscillation of Division Inhibitor MinC in
            <i>Escherichia coli</i>

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

doi:10.1128/jb.181.20.6419-6424.1999

Cited by 353 publications

(240 citation statements)

References 42 publications

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“…4) at the receding edge of the MinD polar zone (Fu et al ., 2001;Hale et al ., 2001;Shih et al ., 2002). Indeed, the ratio of MinD to MinE is critical to the timing of the oscillation (Raskin and de Boer, 1999b).…”

Section: Modelling Mind Oscillationmentioning

confidence: 99%

MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation

Lutkenhaus¹,

Sundaramoorthy

2003

Molecular Microbiology

111

108

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SummaryThe ATPase activity of MinD is required for it to oscillate between the ends of the cell and spatially regulate cell division in Escherichia coli . It is a member of a functionally diverse subgroup of ATPases which are involved in activities ranging from nitrogen fixation (NifH) to plasmid segregation (ParA). All members of the subgroup have a deviant Walker A motif which contains a conserved 'signature' lysine that characterizes this subgroup. In the NifH homodimer the signature lysines make intermonomer contact with the bound nucleotides indicating a role in ATP hydrolysis. ATP binding to NifH leads to formation of an active dimer that associates with a partner that is also a dimer. Because ATP hydrolysis is coupled to formation of the complex, the complex is only transient. In the presence of ATP MinD binds MinC and goes to the membrane, however, the ATPase is not stimulated and the complex is stable. Subsequent interaction of this complex with MinE, however, leads to ATPase stimulation and release of the Min proteins from the membrane. The sequential interaction of MinD with these two proteins, which is dictated by the membrane, is critical to the oscillatory mechanism involved in spatial regulation of division.

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Section: Modelling Mind Oscillationmentioning

confidence: 99%

MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation

Lutkenhaus¹,

Sundaramoorthy

2003

Molecular Microbiology

111

108

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“…GFP fusions to MinC and MinD, on the other hand, oscillate from pole to pole with a periodicity on the order of 10^60 s [145^147]. The membrane localization and oscillation of MinC depend upon MinD, and both MinC and D appear to oscillate as a complex [146]. Interestingly, the oscillation of MinCD depends on MinE, and the midcell localization of MinE depends on MinD.…”

Section: The Min Systemmentioning

confidence: 99%

Themes and variations in prokaryotic cell division

2000

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Perhaps the biggest single task facing a bacterial cell is to divide into daughter cells that contain the normal complement of chromosomes. Recent technical and conceptual breakthroughs in bacterial cell biology, combined with the flood of genome sequence information and the excellent genetic tools in several model systems, have shed new light on the mechanism of prokaryotic cell division. There is good evidence that in most species, a molecular machine, organized by the tubulin-like FtsZ protein, assembles at the site of division and orchestrates the splitting of the cell. The determinants that target the machine to the right place at the right time are beginning to be understood in the model systems, but it is still a mystery how the machine actually generates the constrictive force necessary for cytokinesis. Moreover, although some cell division determinants such as FtsZ are present in a broad spectrum of prokaryotic species, the lack of FtsZ in some species and different profiles of cell division proteins in different families suggests that there are diverse mechanisms for regulating cell division.

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“…This set of proteins is most often referred to as the Min system, a name that captures its 'systemic essence': the proper function and correct localization pattern arise only when the three proteins are expressed together. In the absence of its partners, each Min protein is in fact homogeneously distributed-MinC (de Boer et al, 1992) and MinE in the cytoplasm (Raskin and de Boer, 1999a), and MinD on the membrane (Raskin and de Boer, 1999a). MinD oscillations arise spontaneously in the presence of MinE (Howard and Kruse, 2005;Kruse et al, 2007): MinD binds to the membrane in the ATP form, MinE binds to MinD on the membrane and catalyzes the ATP hydrolysis to ADP, which causes the release of the MinD/MinE complex from the membrane ( Figure 1A).…”

Section: Introductionmentioning

confidence: 99%

Self‐organized partitioning of dynamically localized proteins in bacterial cell division

Ventura

Sourjik

2011

Molecular Systems Biology

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MinDE-Dependent Pole-to-Pole Oscillation of Division Inhibitor MinC in Escherichia coli

Cited by 353 publications

References 42 publications

MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation

MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation

Themes and variations in prokaryotic cell division

Self‐organized partitioning of dynamically localized proteins in bacterial cell division

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