ftsZ is an essential cell division gene in Escherichia coli

Dai, Kang; Lutkenhaus, Joe

doi:10.1128/jb.173.11.3500-3506.1991

Cited by 269 publications

(244 citation statements)

References 30 publications

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“…A weak promoter within the ftsQ gene, pA, was reported by Yi et al (1985) and by Flärdh et al (1997), using transcriptional fusions, although the corresponding RNA species was not detected by S1 mapping (Aldea et al, 1990). Evidence was presented that suggested that promoters upstream of pQ2 are necessary to achieve sufficient ftsZ expression for cell viability (Dai and Lutkenhaus, 1991), but recent results have made this possibility unlikely (Hara et al, 1997). To test whether ppGpp affected ftsQAZ expression at an untested promoter or at the post-transcriptional level, we assayed the concentration of FtsZ protein in wild-type cells and in two mecillinam-resistant mutants, argS201 and a p lac -relAЈ-bearing strain, both of which have a twofold higher ppGpp concentration (Joseleau-Petit et al, 1994).…”

Section: Discussionmentioning

confidence: 92%

“…Strain VIP205 was specially constructed to separate the chromosomal ftsZ gene from its natural promoters and place it under control of the lac promoter (Palacios et al, 1996). As ftsZ is an essential gene (Dai and Lutkenhaus, 1991), this strain grows only in the presence of the lac operon inducer IPTG.…”

Section: Mecillinam Resistance Via Overexpression Of Ftsq Ftsa and Ftszmentioning

confidence: 99%

“…The FtsZ protein seems to be limiting for cell division. At low levels, cell length is inversely proportional to the FtsZ concentration (Dai and Lutkenhaus, 1991;Té tart and Bouché , 1992;Garrido et al, 1993;Palacios et al, 1996). When FtsZ is in moderate excess, polar septa are formed, giving rise to minicells Garrido et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

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Analysis of the effect of ppGpp on the ftsQAZ operon in Escherichia coli

Navarro

Robin

D’Ari

et al. 1998

Molecular Microbiology

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Section: Discussionmentioning

confidence: 92%

Section: Mecillinam Resistance Via Overexpression Of Ftsq Ftsa and Ftszmentioning

confidence: 99%

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Analysis of the effect of ppGpp on the ftsQAZ operon in Escherichia coli

Navarro

Robin

D’Ari

et al. 1998

Molecular Microbiology

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“…FtsZ is a cytoplasmic protein which, at a particular stage in the Escherichia coli cell cycle, locates to the cell centre, forming a polymeric ring (the Z-ring) around the inner circumference of the cytoplasmic membrane Bi & Lutkenhaus, 1991;Dai & Lutkenhaus, 1991; Den Blaauwen et al, 1999;Pla et al, 1991). Invagination of the division septum then follows the shape of the Z-ring as it reduces in diameter until septation is complete Bi & Lutkenhaus, 1991.…”

Section: Introductionmentioning

confidence: 99%

Dynamic FtsZ polymerization is sensitive to the GTP to GDP ratio and can be maintained at steady state using a GTP-regeneration system

Small

Addinall

2003

Microbiology

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In vitro polymerization of the essential bacterial cell division protein FtsZ, in the presence of GTP, is rapid and transient due to its efficient binding and hydrolysis of GTP. In contrast, the in vivo polymeric FtsZ structure which drives cell division -the Z-ring -is present in cells for extended periods of time whilst undergoing constant turnover of FtsZ. It is demonstrated that dynamic polymerization of Escherichia coli FtsZ in vitro is sensitive to the ratio of GTP to GDP concentration. Increase of GDP concentration in the presence of a constant GTP concentration reduces both the duration of FtsZ polymerization and the initial light-scattering maximum which occurs upon addition of GTP. It is also demonstrated that by use of a GTP-regeneration system, polymers of FtsZ can be maintained in a steady state for up to 85 min, while preserving their dynamic properties. The authors therefore present the use of a GTP-regeneration system for FtsZ polymerization as an assay more representative of the in vivo situation, where FtsZ polymers are subject to a constant, relatively high GTP to GDP ratio. INTRODUCTIONThe FtsZ protein has a fundamental role in bacterial cell division , is highly conserved throughout the eubacteria and appears to be required for division of chloroplasts, some archaea and some mitochondria (Beech et al., 2000;Vitha et al., 2001;Wang & Lutkenhaus, 1996). FtsZ is a cytoplasmic protein which, at a particular stage in the Escherichia coli cell cycle, locates to the cell centre, forming a polymeric ring (the Z-ring) around the inner circumference of the cytoplasmic membrane Bi & Lutkenhaus, 1991;Dai & Lutkenhaus, 1991; Den Blaauwen et al., 1999;Pla et al., 1991). Invagination of the division septum then follows the shape of the Z-ring as it reduces in diameter until septation is complete Bi & Lutkenhaus, 1991. FtsZ is strongly related to a/b-tubulin in terms of threedimensional structure (Lowe & Amos, 1998), the possession of GTPase activity (de Boer et al., 1992;Mukherjee et al., 1993;RayChaudhuri & Park, 1992) and the ability to polymerize in a nucleotide-dependent manner in vitro (Erickson et al., 1996;. Indeed, FtsZ forms a variety of polymeric structures in vitro depending on experimental conditions (Erickson et al., 1996;Lowe & Amos, 1999, 2000Yu & Margolin, 1997); however, all of these represent different arrangements of linear protofilaments.There have been multiple studies of the dynamics of FtsZ polymerization in vitro. In the presence of GDP (Rivas et al., 2000(Rivas et al., , 2001 Sossong et al., 1999) or in the presence of GTP under particular conditions where only single protofilaments are formed (Romberg et al., 2001), polymerization is proposed to be isodesmic. Under conditions where FtsZ forms more complex polymers, polymerization and the GTPase activity are co-operative (Caplan & Erickson, 2003;Mukherjee & Lutkenhaus, 1999;White et al., 2000).The technique of right-angled light-scattering has proved useful for real-time monitoring of FtsZ polymerization (Mingorance et al., 2001;...

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“…The ftsz gene is essential and depletion of FtsZ protein leads to cells unable to divide that instead take on a filamentous morphology (4). During division, rod-shaped bacteria such as Escherichia coli synthesize new hemispherical membrane and cell wall, requiring inward forces.…”

mentioning

confidence: 99%

Nucleotide-dependent conformations of FtsZ dimers and force generation observed through molecular dynamics simulations

Hsin

Gopinathan

Huang

2012

Proc. Natl. Acad. Sci. U.S.A.

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The bacterial cytoskeletal protein FtsZ is a GTPase that is thought to provide mechanical constriction force via an unidentified mechanism. Purified FtsZ polymerizes into filaments with varying structures in vitro: while GTP-bound FtsZ assembles into straight or gently curved filaments, GDP-bound FtsZ forms highly curved filaments, prompting the hypothesis that a difference in the inherent curvature of FtsZ filaments provides mechanical force. However, no nucleotide-dependent structural transition of FtsZ monomers has been observed to support this force generation model. Here, we present a series of all-atom molecular dynamics simulations probing the effects of nucleotide binding on the structure of an FtsZ dimer. We found that the FtsZ-dimer structure is dependent on nucleotidebinding state. While a GTP-bound FtsZ dimer retained a firm monomer-monomer contact, a GDP-bound FtsZ dimer lost some of the monomer-monomer association, leading to a "hinge-opening" event that resulted in a more bent dimer, while leaving each monomer structure largely unaffected. We constructed models of FtsZ filaments and found that a GDP-FtsZ filament is much more curved than a GTP-FtsZ filament, with the degree of curvature matching prior experimental data. FtsZ dynamics were used to estimate the amount of force an FtsZ filament could exert when hydrolysis occurs (20-30 pN per monomer). This magnitude of force is sufficient to direct inward cell-wall growth during division, and to produce the observed degree of membrane pinching in liposomes. Taken together, our data provide molecular-scale insight on the origin of FtsZ-based constriction force, and the mechanism underlying prokaryotic cell division.bacterial cell division | bacterial cytoskeleton | GTP hydrolysis T he bacterial cell-division protein FtsZ, a tubulin homolog and a GTPase, polymerizes into filaments situated underneath the cytoplasmic membrane at the division site (1-3). The ftsz gene is essential and depletion of FtsZ protein leads to cells unable to divide that instead take on a filamentous morphology (4). During division, rod-shaped bacteria such as Escherichia coli synthesize new hemispherical membrane and cell wall, requiring inward forces. While an array of proteins are needed for division to occur (5, 6), FtsZ alone has been demonstrated to be sufficient for generating inward pinching forces on liposomes in vitro (7-10), and is thought to be the source of the constriction force needed for division.How FtsZ generates mechanical force is still unclear, but several models have been proposed (11), one of which is based on the intrinsic nucleotide-dependent bending of FtsZ filaments (12, 13). In the presence of GTP, purified FtsZ assembles into either straight or gently curved filaments with a radius of curvature of approximately 100 nm, while in the presence of GDP, highly curved filaments form with a radius of curvature of approximately 10 nm (12,14,15). Subsequent theoretical modeling demonstrated that the rapid transition between straight and curved FtsZ filaments...

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ftsZ is an essential cell division gene in Escherichia coli

Cited by 269 publications

References 30 publications

Analysis of the effect of ppGpp on the ftsQAZ operon in Escherichia coli

Analysis of the effect of ppGpp on the ftsQAZ operon in Escherichia coli

Dynamic FtsZ polymerization is sensitive to the GTP to GDP ratio and can be maintained at steady state using a GTP-regeneration system

Nucleotide-dependent conformations of FtsZ dimers and force generation observed through molecular dynamics simulations

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