Helical Tubes of FtsZ from Methanococcus jannaschii

Löwe, Jan; Amos, Linda

doi:10.1515/bc.2000.122

Cited by 40 publications

(38 citation statements)

References 37 publications

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“…Sheets of protofilaments have been seen under certain conditions for FtsZ from Methanococcus jannaschii (103,104,134) and from Thermotoga maritima (106). FtsZ from M. tuberculosis forms long, two-stranded filaments, in which the two strands must be connected by some type of regular lateral bond (27,199).…”

Section: Lateral Bonds: Do They Exist?mentioning

confidence: 99%

FtsZ in Bacterial Cytokinesis: Cytoskeleton and Force Generator All in One

Erickson

Anderson

Osawa

2010

Microbiol Mol Biol Rev

557

752

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SUMMARY FtsZ, a bacterial homolog of tubulin, is well established as forming the cytoskeletal framework for the cytokinetic ring. Recent work has shown that purified FtsZ, in the absence of any other division proteins, can assemble Z rings when incorporated inside tubular liposomes. Moreover, these artificial Z rings can generate a constriction force, demonstrating that FtsZ is its own force generator. Here we review light microscope observations of how Z rings assemble in bacteria. Assembly begins with long-pitch helices that condense into the Z ring. Once formed, the Z ring can transition to short-pitch helices that are suggestive of its structure. FtsZ assembles in vitro into short protofilaments that are ∼30 subunits long. We present models for how these protofilaments might be further assembled into the Z ring. We discuss recent experiments on assembly dynamics of FtsZ in vitro, with particular attention to how two regulatory proteins, SulA and MinC, inhibit assembly. Recent efforts to develop antibacterial drugs that target FtsZ are reviewed. Finally, we discuss evidence of how FtsZ generates a constriction force: by protofilament bending into a curved conformation.

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Section: Lateral Bonds: Do They Exist?mentioning

confidence: 99%

FtsZ in Bacterial Cytokinesis: Cytoskeleton and Force Generator All in One

Erickson

Anderson

Osawa

2010

Microbiol Mol Biol Rev

557

752

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“…FtsZ polymers strongly resemble tubulin protofilaments (20,51,107,108,126). The simultaneous elucidation of the structures of FtsZ from the thermophilic archaeon Methanococcus jannaschii (105) and the ␣␤-tubulin heterodimer from bovine brain (133) provided conclusive evidence that FtsZ and tubulin are homologues (164).…”

Section: Polymerizationmentioning

confidence: 99%

Cytokinesis in Bacteria

Errington

Daniel

Scheffers

2003

Microbiol Mol Biol Rev

564

601

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Work on two diverse rod-shaped bacteria, Escherichia coli and Bacillus subtilis, has defined a set of about 10 conserved proteins that are important for cell division in a wide range of eubacteria. These proteins are directed to the division site by the combination of two negative regulatory systems. Nucleoid occlusion is a poorly understood mechanism whereby the nucleoid prevents division in the cylindrical part of the cell, until chromosome segregation has occurred near midcell. The Min proteins prevent division in the nucleoid-free spaces near the cell poles in a manner that is beginning to be understood in cytological and biochemical terms. The hierarchy whereby the essential division proteins assemble at the midcell division site has been worked out for both E. coli and B. subtilis. They can be divided into essentially three classes depending on their position in the hierarchy and, to a certain extent, their subcellular localization. FtsZ is a cytosolic tubulin-like protein that polymerizes into an oligomeric structure that forms the initial ring at midcell. FtsA is another cytosolic protein that is related to actin, but its precise function is unclear. The cytoplasmic proteins are linked to the membrane by putative membrane anchor proteins, such as ZipA of E. coli and possibly EzrA of B. subtilis, which have a single membrane span but a cytoplasmic C-terminal domain. The remaining proteins are either integral membrane proteins or transmembrane proteins with their major domains outside the cell. The functions of most of these proteins are unclear with the exception of at least one penicillin-binding protein, which catalyzes a key step in cell wall synthesis in the division septum

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“…FtsZ is the major protein in the ring, although other proteins necessary for division have been identified in Escherichia coli and other species (1)(2)(3). FtsZ is a homolog of tubulin: both proteins share very similar tertiary structures (4), hydrolyze GTP, and assemble into straight and curved protofilaments (5)(6)(7)(8).…”

mentioning

confidence: 99%

Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching

Stricker

Maddox

Salmon

et al. 2002

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

346

392

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FtsZ, the major cytoskeletal component of the bacterial cell-division machine, assembles into a ring (the Z-ring) that contracts at septation. FtsZ is a bacterial homolog of tubulin, with similar tertiary structure, GTP hydrolysis, and in vitro assembly. We used green fluorescent protein-labeled FtsZ and fluorescence recovery after photobleaching to show that the E. coli Z-ring is extremely dynamic, continually remodeling itself with a half-time of 30 s. ZipA, a membrane protein involved in cell division that colocalizes with FtsZ, was equally dynamic. The Z-ring of the mutant ftsZ84, which has 1͞10 the guanosine triphosphatase activity of wild-type FtsZ in vitro, showed a 9-fold slower turnover in vivo. This finding implies that assembly dynamics are determined primarily by GTP hydrolysis. Despite the greatly reduced assembly dynamics, the ftsZ84 cells divide with a normal cell-cycle time.T he processes involved in bacterial cell division are strikingly different from those involved in eukaryotic cytokinesis. Whereas animal cells use a contractile ring of actin and myosin, bacteria form a ring of FtsZ, a cell division protein found in almost every prokaryotic species. This ring, known as the Z-ring, is attached to the inner membrane and contracts during septation. FtsZ is the major protein in the ring, although other proteins necessary for division have been identified in Escherichia coli and other species (1-3). FtsZ is a homolog of tubulin: both proteins share very similar tertiary structures (4), hydrolyze GTP, and assemble into straight and curved protofilaments (5-8).Although the substructure of the Z-ring is not known, in vitro studies suggest that it is based on protofilaments, perhaps associated into multistranded structures. FtsZ polymerizes into single protofilaments under many in vitro solution conditions. Under other conditions, the protofilaments associate side-byside to form ribbons or sheets (5,7,9). An assembly mixture of single protofilaments hydrolyzes GTP at a rate of five molecules per min per FtsZ (10) in physiological buffer conditions (350 mM KCl, pH 7.5; ref. 11). There is no evidence that FtsZ undergoes dynamic microtubule-like instability. Instead, a model of isodesmic assembly has been proposed in which each GTP hydrolysis event results in fragmentation of the protofilament, followed by nucleotide exchange and reannealing (12). In this model, the guanosine triphosphatase (GTPase) activity would reflect very rapid fragmentation͞reannealing dynamics, in which every subunit is turned over, in the sense of breaking and reforming an interface, five times per minute at steady-state.In rapidly dividing E. coli cells, the Z-ring forms in the center of the cell about 1 to 5 min after division, remains for 15 min, and then quickly constricts to divide the cell (13-15). Although the Z-ring appears static when observed by fluorescence of FtsZ-gfp, it could be exchanging subunits with a cytoplasmic pool. In an attempt to directly investigate the assembly dynamics of FtsZ, we performed fluorescence...

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Helical Tubes of FtsZ from Methanococcus jannaschii

Cited by 40 publications

References 37 publications

FtsZ in Bacterial Cytokinesis: Cytoskeleton and Force Generator All in One

FtsZ in Bacterial Cytokinesis: Cytoskeleton and Force Generator All in One

Cytokinesis in Bacteria

Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching

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