Cell cycle and positional constraints on FtsZ localization and the initiation of cell division in <i>Caulobacter crescentus</i>

Quardokus, Ellen M.; Din, Neena; Brun, Yves V.

doi:10.1046/j.1365-2958.2001.02287.x

Cited by 68 publications

(112 citation statements)

References 46 publications

(63 reference statements)

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“…In E. coli and B. subtilis, FtsZ levels do not change significantly during the cell cycle 70 , which indicates that the activity of FtsZ is cellcycle controlled. By contrast, FtsZ levels in C. crescentus vary dramatically because of proteolysis and resynthesis 71 ; nevertheless, the artificial increase of FtsZ levels at the wrong time in the cell cycle does not trigger Z-ring assembly or change the timing of Z-ring constriction 72 . Finding the source of this cell-cycle control of FtsZ activity remains an important challenge for the future.…”

Section: Cell-cycle Timingmentioning

confidence: 95%

FtsZ and the division of prokaryotic cells and organelles

Margolin

2005

Nat Rev Mol Cell Biol

548

479

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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: Cell-cycle Timingmentioning

confidence: 95%

FtsZ and the division of prokaryotic cells and organelles

Margolin

2005

Nat Rev Mol Cell Biol

548

479

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“…Targeting a late-acting divisome component may be easier for the cell than dismantling an existing cytokinetic ring. Interestingly, Z-ring assembly occurs much earlier during the cell cycle in Caulobacter than in E. coli, perhaps necessitating a target other than FtsZ (Quardokus et al 2001). Alternatively, this strategy may prevent the wasteful disassembly and reassembly of the cell division machinery during periods of transient DNA damage.…”

Section: Is Sula An Outlier?mentioning

confidence: 99%

A DNA damage checkpoint in Caulobacter crescentus inhibits cell division through a direct interaction with FtsW

Modell¹,

Hopkins²,

Laub³

2011

Genes Dev.

123

198

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Following DNA damage, cells typically delay cell cycle progression and inhibit cell division until their chromosomes have been repaired. The bacterial checkpoint systems responsible for these DNA damage responses are incompletely understood. Here, we show that Caulobacter crescentus responds to DNA damage by coordinately inducing an SOS regulon and inhibiting the master regulator CtrA. Included in the SOS regulon is sidA (SOS-induced inhibitor of cell division A), a membrane protein of only 29 amino acids that helps to delay cell division following DNA damage, but is dispensable in undamaged cells. SidA is sufficient, when overproduced, to block cell division. However, unlike many other regulators of bacterial cell division, SidA does not directly disrupt the assembly or stability of the cytokinetic ring protein FtsZ, nor does it affect the recruitment of other components of the cell division machinery. Instead, we provide evidence that SidA inhibits division by binding directly to FtsW to prevent the final constriction of the cytokinetic ring.

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“…Bacillus subtilis, Caulobacter crescentus, Rhizobium meliloti and Streptomyces sp. (Latch & Margolin, 1997 ;Ma et al, 1997 ;McCormick et al, 1994 ;Quardokus et al, 2001 ;Sackett et al, 1998 ;Schwedock et al, 1997 ;Van Wezel et al, 2000 ;Wang & Lutkenhaus, 1993). Many of the studies with ftsZ from other organisms have focused on cloning and expression in E. coli hosts.…”

Section: Introductionmentioning

confidence: 99%

Physiological consequences associated with overproduction of Mycobacterium tuberculosis FtsZ in mycobacterial hosts

et al. 2002

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The ftsZ gene of Mycobacterium tuberculosis H37Rv has been characterized as the first step in determining the molecular events involved in the cell division process in mycobacteria. Western analysis revealed that intracellular levels of FtsZ are growth phase dependent in both M. tuberculosis and Mycobacterium smegmatis. Unregulated expression of M. tuberculosis ftsZ from constitutive hsp60 and dnaA promoters in M. tuberculosis hosts resulted in lethality whereas expression from only the hsp60 promoter was toxic in M. smegmatis hosts. Expression of ftsZ from the dnaA promoter in M. smegmatis resulted in "sixfold overproduction and the merodiploids exhibited slow growth, an increased tendency to clump and filament, and in some cases produced buds and branches. Many of the cells also contained abnormal and multiple septa.

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Cell cycle and positional constraints on FtsZ localization and the initiation of cell division in Caulobacter crescentus

Cited by 68 publications

References 46 publications

FtsZ and the division of prokaryotic cells and organelles

FtsZ and the division of prokaryotic cells and organelles

A DNA damage checkpoint in Caulobacter crescentus inhibits cell division through a direct interaction with FtsW

Physiological consequences associated with overproduction of Mycobacterium tuberculosis FtsZ in mycobacterial hosts

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