Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein

RayChaudhuri, Debabrata; Park, James T.

doi:10.1038/359251a0

Cited by 411 publications

(340 citation statements)

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“…This study pointed out that GTP hydrolysis may induce a structural change at the nucleotide interface by pushing against the T7-loop region of the adjacent monomer. The high turnover of GTP that FtsZ displays in solution seems not to be critical for functioning, since this work and previous reports describe FtsZ mutants that are capable of in vivo and/or in vitro assembly with severely inhibited GTP-hydrolysis activity (11,12,30,40). Although most of the T7-loop mutants interact with wt protein, they do not readily assemble into polymers, indicating that the interface may be critical for the formation of FtsZ polymers.…”

Section: Discussionmentioning

confidence: 49%

GTP Hydrolysis of Cell Division Protein FtsZ: Evidence that the Active Site Is Formed by the Association of Monomers

et al. 2001

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The essential prokaryotic cell division protein FtsZ is a tubulin homologue that forms a ring at the division site. FtsZ forms polymers in a GTP-dependent manner. Recent biochemical evidence has shown that FtsZ forms multimeric structures in vitro and in vivo and functions as a self-activating GTPase. Structural analysis of FtsZ points to an important role for the highly conserved tubulin-like loop 7 (T7-loop) in the self-activation of GTP hydrolysis. The T7-loop was postulated to form the active site together with the nucleotide-binding site on an adjacent FtsZ monomer. To characterize the role of the T7-loop of Escherichia coli FtsZ, we have mutagenized residues M206, N207, D209, D212, and R214. All the mutant proteins, except the R214 mutant, are severely affected in polymerization and GTP hydrolysis. Charged residues D209 and D212 cannot be substituted with a glutamate residue. All mutants interact with wildtype FtsZ in vitro, indicating that the T7-loop mutations do not abolish FtsZ self-association. Strikingly, in mixtures of wild-type and mutant proteins, most mutants are capable of inhibiting wild-type GTP hydrolysis. We conclude that the T7-loop is part of the active site for GTP hydrolysis, formed by the association of two FtsZ monomers.

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Section: Discussionmentioning

confidence: 49%

GTP Hydrolysis of Cell Division Protein FtsZ: Evidence that the Active Site Is Formed by the Association of Monomers

et al. 2001

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“…Like tubulin, purified FtsZ binds and hydrolyses GTP [14][15][16] . GTP binding induces FtsZ self-assembly into protofilaments that consist of a head-to-tail linear polymer of FtsZ 10,[17][18][19] .…”

Section: Structure and Assembly Of Ftszmentioning

confidence: 99%

FtsZ and the division of prokaryotic cells and organelles

Margolin

2005

Nat Rev Mol Cell Biol

560

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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“…A band with the apparent molecular weight of 46 kDa is detected in the first four lanes only. The inferred molecular weight of FtsZ is 41 kDa, but FtsZ proteins can run slowly on SDS-PAGE (RayChaudhuri and Park, 1992). with the rings observed by electron microscopy (Bi and Lutkenhaus, 1991) appearing as lines or stripes perpendicular to the long axis of the cell when viewed from the side by immunofluorescence microscopy (Levin and Losick, 1996). We anticipated that FtsZ rings would be rare in substrate mycelium, with its sporadic cross-walls, but frequent in aerial hyphae.…”

Section: Visualization Of Ftsz By Immunofluorescence Microscopymentioning

confidence: 99%

“…FtsZ is a tubulin-like protein that polymerizes in a GTP-dependent manner to form a ring at the site of incipient septation (de Boer et al, 1992;RayChaudhuri and Park, 1992;Bramhill and Thompson, 1994;Mukherjee and Lutkenhaus, 1994). It plays a pivotal role in the process of cytokinesis in bacteria, and homologues of FtsZ have been found in all prokaryotes that have been investigated for its presence (Lutkenhaus, 1993;Dharmatilake and Kendrick, 1994;McCormick et al, 1994;Baumann and Jackson, 1996;Bult et al, 1996;Margolin et al, 1996;Quardokus et al, 1996;Wang and Lutkenhaus, 1996).…”

Section: Introductionmentioning

confidence: 99%

Assembly of the cell division protein FtsZ into ladder‐like structures in the aerial hyphae of Streptomyces coelicolor

Schwedock

McCormick

Angert

et al. 1997

Molecular Microbiology

131

134

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SummaryIn the filamentous bacterium Streptomyces coelicolor, the cell division protein FtsZ is required for the conversion of multinucleoidal aerial hyphae into chains of uninucleoidal spores, although it is not essential for viability. Using immunofluorescence microscopy, we have shown that FtsZ assembles into long, regularly spaced, ladder-like arrays in developing aerial hyphae, with an average spacing of about 1.3 m. Within individual hyphae, ladder formation was relatively synchronous and extended for distances over 100 m. These ladders were present only transiently, decreasing in intensity as chromosomes separated into distinct nucleoids and disappearing upon the completion of septum formation. Evidence from the overall intensity of immunofluorescence staining suggested that ladder formation was regulated in part at the level of the accumulation and degradation of FtsZ within individual aerial hyphae. Finally, FtsZ ladder formation was under developmental control in that long arrays of FtsZ rings could not be detected in certain so-called white mutants (whiG, whiH and whiB ), which are blocked in spore formation. The assembly of FtsZ into ladders represents the earliest known molecular manifestation of the process of spore formation, and its discovery provides insight into the role of whi genes in the conversion of aerial hyphae into chains of spores. We have also described a novel use of a cell wall-staining technique to visualize apical tip growth in vegetatively growing hyphae.

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Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein

Cited by 411 publications

References 35 publications

GTP Hydrolysis of Cell Division Protein FtsZ: Evidence that the Active Site Is Formed by the Association of Monomers

GTP Hydrolysis of Cell Division Protein FtsZ: Evidence that the Active Site Is Formed by the Association of Monomers

FtsZ and the division of prokaryotic cells and organelles

Assembly of the cell division protein FtsZ into ladder‐like structures in the aerial hyphae of Streptomyces coelicolor

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