AAA+ Chaperone ClpX Regulates Dynamics of Prokaryotic Cytoskeletal Protein FtsZ

Sugimoto, Shinya; Yamanaka, Kunitoshi; Nishikori, Shingo; Miyagi, Atsushi; Ando, Toshio; Ogura, Teru

doi:10.1074/jbc.m109.080739

Cited by 45 publications

(49 citation statements)

References 43 publications

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“…Imaging rate, 1.03 fps (×20 playback); scan size, 800 × 800 nm 2 [98]. ・Crystallization of a CaCO 3 thin film from supersaturated solution [72] ・Ultrafast imaging of collagen [58] ・Brownian motion & photo-degradation of π-conjugated polyrotaxane [73] ・DNA translocation and looping by type III restriction enzyme [74] ・Biotinylated DNA-streptavidin interaction [75] Miles Miles Shinohara Takeyasu Trimitsu 2008 5 ・Anisotropic diffusion of point defects in streptavidin 2D crystals [76] ・Identification of intrinsically disordered regions of proteins [77] ・Human chromosomes in liquid [78] ・DNA-nuclease interaction [ ・Dynamic equilibrium at the edge of bR 2D crystals [81] ・Structural change of CaM and actin polymerization on streptavidin 2D crystals [82] ・Unidirectional translocation of cellulase along cellulose fibers [83] ・Translocation of EcoRII restriction enzyme along DNA [84] ・Fabrication and imaging of hard material surface [85] ・Purple membrane in contact-mode HS-AFM [86] ・Thermal motion of π-conjugated polymer chain [87] ・Opening of 3D hollow structure of DNA Origami [88] ・Opening of 3D hollow structure of DNA Origami [89] ・ATP-induced conformational change in P2X 4 ・Walking myosin V along an actin filament [91] ・Photo-induced structural change in bR [92] ・2D crystal formation of annexin A-V and height change of p97 [93] ・Analysis of components covering magnesotome surface [94] ・Time course of cell death by antimicrobial peptide [95] ・Dissolution of extreme UV exposed resist films under developing [96] ・Dissolution of extreme UV exposed resist films under developing [97] ・Process of forming supported planar lipid bilayer [98] ・Self assembly of amyloid-like fibrils [99] ・Effect of ClpX on FtsZ polymerization ...…”

Section: Resultsmentioning

confidence: 99%

High-speed atomic force microscopy coming of age

Ando¹

2012

Nanotechnology

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High-speed atomic force microscopy (HS-AFM) is now materialized. It allows direct visualization of dynamic structural changes and dynamic processes of functioning biological molecules in physiological solutions, at high spatiotemporal resolution. Dynamic molecular events unselectively appear in detail in an AFM movie, facilitating our understanding of how biological molecules operate to function. This review describes a historical overview of technical development towards HS-AFM, summarizes elementary devices and techniques used in the current HS-AFM, and then highlights recent imaging studies. Finally, future challenges of HS-AFM studies are briefly discussed.

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Section: Resultsmentioning

confidence: 99%

High-speed atomic force microscopy coming of age

Ando¹

2012

Nanotechnology

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314

246

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“…The same study showed that ClpXP degrades both FtsZ monomers and polymers in vitro (11). In a subsequent study it was reported that overexpression of either full-length ClpX or the N-terminal substrate binding domain of ClpX to very high levels causes filamentation and perturbs formation of the FtsZ ring in a wild-type background (34). It was also reported that in vitro ClpX could inhibit FtsZ polymerization by an ATP-and ClpP-independent mechanism (34).…”

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confidence: 91%

“…An additional regulator of FtsZ that has been identified is ClpX (11,34,38). ClpX is a member of the AAAϩ (ATPases associated with various cellular activities) family of ATPases and forms a complex with ClpP, a serine protease.…”

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The Interplay of ClpXP with the Cell Division Machinery in Escherichia coli

2011

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ClpXP is a two-component protease composed of ClpX, an ATP-dependent chaperone that recognizes and unfolds specific substrates, and ClpP, a serine protease. One ClpXP substrate in Escherichia coli is FtsZ, which is essential for cell division. FtsZ polymerizes and forms the FtsZ ring at midcell, where division occurs. To investigate the role of ClpXP in cell division, we examined the effects of clpX and clpP deletions in several strains that are defective for cell division. Together, our results suggested that ClpXP modulates cell division through degradation of FtsZ and possibly other cell division components that function downstream of FtsZ ring assembly. In the ftsZ84 strain, which is temperature sensitive for filamentation due to a mutation in ftsZ, we observed that deletion of clpX or clpP suppresses filamentation and reduces FtsZ84 degradation. These results are consistent with ClpXP playing a role in cell division by modulating the level of FtsZ through degradation. In another division-defective strain, ⌬minC, the additional deletion of clpX or clpP delays cell division and exacerbates filamentation. Our results demonstrate that ClpXP modulates division in cells lacking MinC by a mechanism that requires ATP-dependent degradation. However, antibiotic chase experiments in vivo indicate that FtsZ degradation is slower in the ⌬minC strain than in the wild type, suggesting there may be another cell division component degraded by ClpXP. Taken together these studies suggest that ClpXP may degrade multiple cell division proteins, thereby modulating the precise balance of the components required for division.

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“…Also, even in mycobacteria, FtsW is apparently a late recruit to the Z ring (54,155), so something else must provide the primary membrane tether. Several other proteins that regulate the Z ring (reviewed in reference 2) bind to this C-terminal peptide of FtsZ: EzrA (175), SepF (176), ClpX (25,185), and the C-terminal domain of MinC (170). EzrA is probably the best candidate for a tether, because it is a transmembrane protein with a topology like that of ZipA (96).…”

Section: Tethering Ftsz To the Membranementioning

confidence: 99%

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

Erickson

Anderson

Osawa

2010

Microbiol Mol Biol Rev

541

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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AAA+ Chaperone ClpX Regulates Dynamics of Prokaryotic Cytoskeletal Protein FtsZ

Abstract: AAA

Cited by 45 publications

References 43 publications

High-speed atomic force microscopy coming of age

High-speed atomic force microscopy coming of age

The Interplay of ClpXP with the Cell Division Machinery in Escherichia coli

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

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