Structural Insights into the Conformational Variability of FtsZ

Oliva, M.A.; Trambaiolo, Daniel; Löwe, Jan

doi:10.1016/j.jmb.2007.08.056

Cited by 161 publications

(184 citation statements)

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“…In tubulin, this loop is composed of 13 residues (1-3). The corresponding loop is much shorter in FtsZ proteins, consistent with the fact that FtsZ does not form tubulin microtubule-like structures (5,(28)(29)(30). In TubZ, the M loop is even shorter than in FtsZ, spanning only four residues.…”

Section: Resultssupporting

confidence: 62%

“…4B). Database searches showed that TubZ indeed belongs to the tubulin/FtsZ family of proteins and is similar to both eukaryotic and prokaryotic members of the family; TubZ can be optimally superimposed with rmsds of 3.4 Å onto both bovine α tubulin and Pseudomonas aeruginosa FtsZ (1,5). Whereas the two-domain architectures of tubulin, FtsZ, and TubZ are similar in overall structure, the extreme N-and C-terminal regions of these proteins are very divergent (Fig.…”

Section: Resultsmentioning

confidence: 97%

“…Tubulin proteins do not contain significant N-terminal extensions, whereas FtsZ proteins from different organisms show structural variability within their N-terminal regions. For instance, in the Escherichia coli FtsZ structure the N-terminal residues are disordered, whereas Methanococcus jannaschii FtsZ has an extra N-terminal helix, H0, which is flexibly attached to the body of the protein and has been captured in multiple orientations (5). Although H0 is not conserved in FtsZ proteins, one M. jannaschii FtsZ structure revealed a semicontinuous polymer in the crystal, thought to closely represent in vivo protofilaments, which utilizes H0 in subunit-subunit contacts (4).…”

Section: Resultsmentioning

confidence: 99%

“…However, unlike tubulin, FtsZ does not function in DNA segregation but rather cell division. Specifically, it forms a cytokinetic ring called the Z ring at midcell, which mediates septation (5,6). Recently, however, prokaryotic proteins encoded on large plasmids harbored in bacilli showing 15-20% sequence similarity to both FtsZ and tubulin have been identified and dubbed TubZ (7)(8)(9)(10)(11)(12).…”

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confidence: 99%

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Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition

Kumaraswami

et al. 2010

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

101

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The segregation of plasmid DNA typically requires three elements: a DNA centromere site, an NTPase, and a centromere-binding protein. Because of their simplicity, plasmid partition systems represent tractable models to study the molecular basis of DNA segregation. Unlike eukaryotes, which utilize the GTPase tubulin to segregate DNA, the most common plasmid-encoded NTPases contain Walker-box and actin-like folds. Recently, a plasmid stability cassette on Bacillus thuringiensis pBtoxis encoding a putative FtsZ/tubulin-like NTPase called TubZ and DNA-binding protein called TubR has been described. How these proteins collaborate to impart plasmid stability, however, is unknown. Here we show that the TubR structure consists of an intertwined dimer with a winged helix-turn-helix (HTH) motif. Strikingly, however, the TubR recognition helices mediate dimerization, making canonical HTH-DNA interactions impossible. Mutagenesis data indicate that a basic patch, encompassing the two wing regions and the N termini of the recognition helices, mediates DNA binding, which indicates an unusual HTH-DNA interaction mode in which the N termini of the recognition helices insert into a single DNA groove and the wings into adjacent DNA grooves. The TubZ structure shows that it is as similar structurally to eukaryotic tubulin as it is to bacterial FtsZ. TubZ forms polymers with guanine nucleotide-binding characteristics and polymer dynamics similar to tubulin. Finally, we show that the exposed TubZ C-terminal region interacts with TubR-DNA, linking the TubR-bound pBtoxis to TubZ polymerization. The combined data suggest a mechanism for TubZ-polymer powered plasmid movement.

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Section: Resultssupporting

confidence: 62%

Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition

Kumaraswami

et al. 2010

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

101

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“…In recent years, it has been reported that in some FtsZ-mutant cells, even when there is no detectable GTPase activity, the mutant cells can still show cell division ability and take the physiological role of division. For this reason, the hydrolysis reaction of GTP is not considered as the only energy source for the construction of the septum but is regarded as a promotive element in the symmetric invagination of cell division [62,63].…”

Section: Function and Dynamicsmentioning

confidence: 99%

Small molecules targeting at the bacterial cell division protein FtsZ as potential antimicrobial agents

Sun¹,

Wong²

2018

Fighting Antimicrobial Resistance

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Bacterial Cell Division

Natale

Vicente

2020

Encyclopedia of Life Sciences

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Escherichia coli assembles a contractile ring, the divisome, in its envelope at the middle of its length exactly when it is needed for division. Its main component, FtsZ, is a cytoplasmic protein lacking the ability to be positioned by itself in the membrane. Additional proteins regulate either the action, the positioning or the stability of FtsZ by interacting with a unique region called the FtsZ ‘central hub’. The assembly of the divisome is initiated by a proto‐ring, in which ZipA and FtsA are two proteins that use the central hub for attaching FtsZ to the membrane. Polymerisation of FtsZ is blocked at the poles by the MinCDE proteins and also prevented by SlmA to occur at places adjacent to the nucleoid. After nucleoid segregation, the divisome becomes functional at midcell where it triggers invagination of the membrane and the production of septal peptidoglycan, leading ultimately to an efficient cell division. Key Concepts Division depends on a cytoskeletal element (FtsZ ring) that functions as a scaffold to recruit additional division proteins. Spatial regulation of the FtsZ‐ring placement involves positioning inhibitors of FtsZ in the cell to prevent FtsZ polymers from assembling at the poles or across unsegregated nucleoids. Several complexes that effect the division process localise at specific places of the cell at precise moments after growth and nucleoid segregation. The interactions of FtsZ, a cytoplasmic protein, with the proto‐ring anchors, FtsA and ZipA, serve to associate it to the cytoplasmic membrane forming the proto‐ring, the initial precursor of the division machinery. The central hub of FtsZ is key to the action of the FtsZ regulatory proteins FtsA, FtsE, FtsX, ZipA, ZapC, ZapD, MinC, SlmA and ClpX. The Min proteins generate an oscillatory pattern in artificial systems, and FtsZ filaments can form rings when attached to a lipid bilayer that has a cylindrical shape. PBP3‐independent peptidoglycan synthesis (PIPS) prior to the production of septal peptidoglycan directly connects cytoplasmic division proteins with peptidoglycan synthesis in the bacterial periplasm.

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Structural Insights into the Conformational Variability of FtsZ

Cited by 161 publications

References 50 publications

Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition

Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition

Small molecules targeting at the bacterial cell division protein FtsZ as potential antimicrobial agents

Bacterial Cell Division

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