Concentration and Assembly of the Division Ring Proteins FtsZ, FtsA, and ZipA during the<i>Escherichia coli</i>Cell Cycle

Rueda, Sonsoles; Vicente, Miguel; Mingorance, Jesús

doi:10.1128/jb.185.11.3344-3351.2003

Cited by 194 publications

(197 citation statements)

References 51 publications

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“…For a single E. coli cell, there are nearly 15,000 copies of FtsZ and in the entire cell cycle the FtsZ concentration almost remains constant [30,46]. Interestingly, at a given time, there are only about 30 % of FtsZ taking part in the Z-ring formation.…”

Section: Function and Dynamicsmentioning

confidence: 99%

“…The function of FtsZ is to polymerize to form Z-ring for controlling the division of a bacterial mother cell into daughter cells [26,28,29]. Furthermore, just as the microtubule assembly is influenced by microtubule associated proteins, the stability of FtsZ polymerization is controlled in vivo by bacterial cell division proteins such as FtsA, ZipA, and ZapA [28,[30][31][32][33][34].…”

Section: The Structurementioning

confidence: 99%

“…Therefore, the resulting Z-ring is a dynamic structure balanced between assembly and disassembly [49]. The FtsZ assembly process is started under the conditions that separation of nucleoids and replication of DNA are completed [30], and the required GTP concentration is above a critical concentration of 0.5-1 μM [50][51][52]. When these external conditions are realized, FtsZ monomers bind with GTP and undergo cooperatively assembly in a head-to-tail manner to form protofilaments that are straight single-stranded protein filaments (4-5 nm in width) [53].…”

Section: Function and Dynamicsmentioning

confidence: 99%

See 2 more Smart Citations

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

Sun¹,

Wong²

2018

Fighting Antimicrobial Resistance

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Section: Function and Dynamicsmentioning

confidence: 99%

Section: The Structurementioning

confidence: 99%

Section: Function and Dynamicsmentioning

confidence: 99%

See 1 more Smart Citation

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

Sun¹,

Wong²

2018

Fighting Antimicrobial Resistance

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“…Hydrolysis of the bound nucleotide leads to depolymerization of the FtsZ protofilaments (Erickson et al, 2010;Mukherjee & Lutkenhaus, 1998). As FtsZ levels are essentially constant throughout the cell cycle, spatiotemporal control of division is exercised largely through the assembly/ disassembly of the Z-ring (Rueda et al, 2003;Weart & Levin, 2003). A number of proteins that interact with FtsZ contribute to its function by modulating the dynamics of FtsZassembly (Adams & Errington, 2009;Huang et al, 2013;Lutkenhaus et al, 2012;Ortiz et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

ClpXP and ClpAP control the Escherichia coli division protein ZapC by proteolysis

2016

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The bacterial FtsZ-ring is an essential cytokinetic structure under tight spatiotemporal regulation. In Escherichia coli, FtsZ polymerization and assembly into the Z-ring is controlled on multiple levels through interactions with positive and negative regulators. Among these regulatory factors are ZapC, a Z-ring stabilizer, and the conserved protease ClpXP, which has been shown to degrade FtsZ protofilaments in preference to FtsZ monomers. Here we report that ZapC and ClpX interact in a protein-protein interaction assay, and that ZapC is degraded in a ClpXP-dependent manner in vivo. The SspB adaptor protein is not required for targeting ZapC to the ClpXP proteolytic machinery. A mutation disrupting the zapC ssrAlike sequence (zapC DD ) stabilizes ZapC consistent with a reduction in ClpXP-mediated ZapC degradation. ZapC DD retains the ability to interact with FtsZ and to promote bundling in vitro indicating that WT ZapC contains discrete FtsZ and ClpX recognition motifs. Additionally, ClpAP complexes are sufficient for degradation of ZapC in the absence of ClpX in vivo. Further, chromosomal expression of zapC DD suppresses filamentation of the temperature-sensitive ftsZ84 mutant, confirming the role of ZapC as a Z-ring stabilizer. Lastly, changes in ClpXP and ZapC levels lead to cell division effects, likely through their roles in modulating FtsZ assembly dynamics. Taken together, our results indicate that the Zring stabilizer ZapC is a substrate of both ClpXP and ClpAP in vivo. Our data also point to a more complex regulatory circuit that integrates FtsZ, ClpXP and ZapC in achieving Z-ring stability in E. coli and related species.

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“…Known fts mutants include ftsA, ftsI, ftsK, ftsL, ftsN, ftsW and ftsZ. [1][2][3][4][5][6][7][8] Inhibitors of protein synthesis exhibit bacteriostatic action except for the aminoglycoside (AG) antibiotics, 9) suggesting that the inhibition of protein synthesis by AG antibiotics is not directly involved in their bactericidal action. The bactericidal action of AG antibiotic is assumed to be based on their inhibition of DNA replication.…”

mentioning

confidence: 99%

Inhibition of Septation in Bacillus subtilis by a Peptide Antibiotic, Edeine B1

Shimotohno

Kawamura

Natori

et al. 2010

Biological & Pharmaceutical Bulletin

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The antibiotics, edeine A 1 and B 1 , are well-known inhibitors of protein biosynthesis in both prokaryote and eukaryote cells. Edeine A 1 and B 1 show almost the same biological activity. We show herein that edeine B 1 exhibits a lethal action in Bacillus subtilis, inhibiting septation via a mechanism different from the inhibition of protein synthesis by this antibiotic.The complex process of cell division is closely interconnected with other cellular processes. Chromosomal DNA replication, nuclear division, and cell division must be coordinated in time and space. DNA metabolism plays a pivotal role in the cell division events controlled by the partitioning of newly replicated chromosomes to daughter cells. This involves chromosomal DNA replication, the positioning of a septum at the midpoint of the cell, the assembly of cytoskeletal elements, and the cleavage of the septum after chromosome segregation. Genetic studies have unraveled the process of cell division by the analysis of filamenting temperaturesensitive mutants. In prokaryotes, filamenting temperaturesensitive (fts) genes produce the proteins essential for cell division. Known fts mutants include ftsA, ftsI, ftsK, ftsL, ftsN, ftsW and ftsZ. [1][2][3][4][5][6][7][8] Inhibitors of protein synthesis exhibit bacteriostatic action except for the aminoglycoside (AG) antibiotics, 9) suggesting that the inhibition of protein synthesis by AG antibiotics is not directly involved in their bactericidal action. The bactericidal action of AG antibiotic is assumed to be based on their inhibition of DNA replication. AG antibiotic blocks the initiation of DNA replication, 10) and interrupts oriC-membrane attachment. 11) The oriC-membrane attachment [12][13][14] is crucial for subsequent initiation of DNA replication, chromosome segregation, and septation of bacterial cells. Blocking DNA replication is known to lead to the save our ships (SOS) response in Escherichia coli, thereby inhibiting cell division. 15) We demonstrate herein that edeine B 1 inhibits cell division, exerting its bactericidal action by inhibiting FtsZ assembly, independently of its inhibitory effect on protein synthesis. MATERIALS AND METHODSPurification of Edeine B 1 Edeine B 1 was isolated from a culture filtrate of Bacillus brevis TTO2-8. The purified edeine B 1 yielded a single TLC spot, a single HPLC peak and the predicted structure based on NMR and FAB-MAS analysis. Edeine B 1 is a linear basic oligopeptide antibiotic consisting of five amino acid residues (isotyrosine, isoserine, a,b-diaminopropionic acid, 2,6-diamino-7-hydroxyazelanic acid, and glycine) and an organic base (guanylspermidine) produced by B. brevis. 16,17) Bacterial Strains B. subtilis 168 and mutant FtsZ ts1 (a temperature sensitive mutant of B. subtilis 168) were used.Viable Cell Number The viable cell number was counted by plating on LB (Luria-Bertani) agar, and recording the number of colonies that developed after 24 h incubation.Western Blotting Anti-FtsZ rabbit antibody raised against a chemically synthesized carboxyl t...

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Concentration and Assembly of the Division Ring Proteins FtsZ, FtsA, and ZipA during theEscherichia coliCell Cycle

Cited by 194 publications

References 51 publications

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

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

ClpXP and ClpAP control the Escherichia coli division protein ZapC by proteolysis

Inhibition of Septation in Bacillus subtilis by a Peptide Antibiotic, Edeine B1

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