Ftsz Ring Formation at the Chloroplast Division Site in Plants

Vitha, Stanislav; McAndrew, Rosemary S.; Osteryoung, Katherine W.

doi:10.1083/jcb.153.1.111

Cited by 256 publications

(294 citation statements)

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“…The functioning of a cooperative mechanism of FtsZ polymerization has been proposed as well by others (14, 38 -40). 2 In contrast, in the presence of GDP most of the FtsZ protein (over 98%) was recovered in the soluble fraction as would be expected if the dimer were the most abundant form of the GDP-bound FtsZ in solution (see above, Fig. 1).…”

Section: Ftsz In Its Gdp-bound State In Physiological Buffer Has Amentioning

confidence: 89%

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Essential Cell Division Protein FtsZ Assembles into One Monomer-thick Ribbons under Conditions Resembling the Crowded Intracellular Environment

González

Jiménez

Vélez

et al. 2003

Journal of Biological Chemistry

173

227

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Experimental conditions that simulate the crowded bacterial cytoplasmic environment have been used to study the assembly of the essential cell division protein FtsZ from Escherichia coli. In solutions containing a suitable concentration of physiological osmolytes, macromolecular crowding promotes the GTP-dependent assembly of FtsZ into dynamic two-dimensional polymers that disassemble upon GTP depletion. Atomic force microscopy reveals that these FtsZ polymers adopt the shape of ribbons that are one subunit thick. When compared with the FtsZ filaments observed in vitro in the absence of crowding, the ribbons show a lag in the GTPase activity and a decrease in the GTPase rate and in the rate of GTP exchange within the polymer. We propose that, in the crowded bacterial cytoplasm under assembly-promoting conditions, the FtsZ filaments tend to align forming dynamic ribbon polymers. In vivo these ribbons would fit into the Z-ring even in the absence of other interactions. Therefore, the presence of mechanisms to prevent the spontaneous assembly of the Z-ring in non-dividing cells must be invoked.

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Section: Ftsz In Its Gdp-bound State In Physiological Buffer Has Amentioning

confidence: 89%

“…The FtsZ protein is conserved in most of the prokaryotic organisms and several organelles and plays a central role in microbial and organelle division forming a ring at the division site (1,2). It is structurally related to the eukaryotic cytoskeletal tubulin (3,4), binds guanine nucleotides, and has GTPase activity (5)(6)(7).…”

mentioning

confidence: 99%

Essential Cell Division Protein FtsZ Assembles into One Monomer-thick Ribbons under Conditions Resembling the Crowded Intracellular Environment

González

Jiménez

Vélez

et al. 2003

Journal of Biological Chemistry

173

227

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“…An extensive network of filamentous structures is formed by FtsZ-GFP and a similar network is observed in electron micrographs 115 . This array, however, is not detected by immunostaining and might be an artefact of abnormally high expression levels 107 . Interestingly, in moss, one isoform of FtsZ can localize as rings in both chloroplasts and in the host-cell cytoplasm as detected by GFP fusions or by immunofluorescence 116 , which indicates that it might have a role in division of the host cell.…”

Section: Ftsz and Organelle Division Plastid Divisionmentioning

confidence: 97%

“…They are found in the STROMAL COMPARTMENT and co-localize to a ring structure at the midpoint of the chloroplast 107 . An additional homologue of FtsZ that is distinct from FtsZ1 and FtsZ2, but is still related to cyanobacterial FtsZs, is also present in plastids of primitive algae.…”

Section: Ftsz and Organelle Division Plastid Divisionmentioning

confidence: 99%

FtsZ and the division of prokaryotic cells and organelles

Margolin

2005

Nat Rev Mol Cell Biol

548

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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“…The 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).…”

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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Ftsz Ring Formation at the Chloroplast Division Site in Plants

Cited by 256 publications

References 49 publications

Essential Cell Division Protein FtsZ Assembles into One Monomer-thick Ribbons under Conditions Resembling the Crowded Intracellular Environment

Essential Cell Division Protein FtsZ Assembles into One Monomer-thick Ribbons under Conditions Resembling the Crowded Intracellular Environment

FtsZ and the division of prokaryotic cells and organelles

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

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