The<i>Escherichia coli</i>FtsK functional domains involved in its interaction with its divisome protein partners

Grenga, Lucia; Luzi, G.; Paolozzi, L.; Ghelardini, P.

doi:10.1111/j.1574-6968.2008.01317.x

Cited by 25 publications

(29 citation statements)

References 17 publications

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“…The bifunctional nature of FtsK makes it an intriguing cell division checkpoint candidate, as it is proposed to sense both proper DNA segregation and complete accumulation of divisome proteins within the same molecule (17,24). Previous biochemical evidence suggests that FtsK N interacts with both cytoplasmic and membrane-bound proteins within the divisome (17,25,26). These include the major cell division protein FtsZ, a homolog of the eukaryotic cytoskeletal protein tubulin that forms the dynamic ring-like structure at the division site known as the Z-ring (27)(28)(29)(30), and proteins involved in peptidoglycan synthesis, such as FtsQ, FtsL, and FtsI (31)(32)(33)(34)(35)(36)(37).…”

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confidence: 99%

Site-directed Fluorescence Labeling Reveals a Revised N-terminal Membrane Topology and Functional Periplasmic Residues in the Escherichia coli Cell Division Protein FtsK

Berezuk

Goodyear

Khursigara

2014

Journal of Biological Chemistry

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Background:FtsK is an essential membrane protein that links chromosome segregation and cell division in bacteria. Results: A revised membrane topology of FtsK highlights a large functional periplasmic loop. Conclusion: Key residues in the newly identified periplasmic loop of FtsK couple division of the cytoplasmic and outer membranes. Significance: FtsK functions as a critical checkpoint for the transition between cell growth and septation.

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confidence: 99%

Site-directed Fluorescence Labeling Reveals a Revised N-terminal Membrane Topology and Functional Periplasmic Residues in the Escherichia coli Cell Division Protein FtsK

Berezuk

Goodyear

Khursigara

2014

Journal of Biological Chemistry

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“…Furthermore, the presence of gfp at the attTn7 site did not alter the growth constant compared to that of the Str r strain (Table 4). Microscopic examination and flow cytometry analysis of Str-GFP and Nal-GFP cells did not show the cell elongation that would be expected when a region important to FtsK function is perturbed (37) (Fig. 2A).…”

Section: Sequencing Results and Comparative Analysis Of Genomesmentioning

confidence: 99%

“…Flow cytometry analysis. GFP-labeled Str r (Str-GFP) and Nal r (Nal-GFP) clones were analyzed using flow cytometry to detect cell division and/or chromosome segregation defects (37). To analyze cell division, overnight cultures were subcultured in 3 ml LB with a 1:100 dilution in 15 ml tubes with and without 15 g/ml ampicillin and grown for 3 h with shaking at 37°C.…”

Section: Methodsmentioning

confidence: 99%

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In Vitro Evolution of an Archetypal Enteropathogenic Escherichia coli Strain

et al. 2013

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Enteropathogenic Escherichia coli (EPEC) is a leading cause of infantile diarrhea in developing countries. EPEC strain E2348/69 is used worldwide as a prototype to study EPEC genetics and disease. However, isolates of E2348/69 differ phenotypically, reflecting a history of in vitro selection. To identify the genomic and phenotypic changes in the prototype strain, we sequenced the genome of the nalidixic acid-resistant (Nal r ) E2348/69 clone. We also sequenced a recent nleF mutant derived by one-step PCR mutagenesis from the Nal r strain. The sequencing results revealed no unintended changes between the mutant and the parent strain. However, loss of the pE2348-2 plasmid and 3 nonsynonymous mutations were found in comparison to the published streptomycin-resistant (Str r ) E2348/69 reference genome. One mutation is a conservative amino acid substitution in ftsK. Another, in gyrA, is a mutation known to result in resistance to nalidixic acid. The third mutation converts a stop codon to a tryptophan, predicted to result in the fusion of hflD, the lysogenization regulator, to purB. The purB gene encodes an adenylosuccinate lyase involved in purine biosynthesis. The Nal r clone has a lower growth rate than the Str r isolate when cultured in minimal media, a difference which is corrected upon addition of adenine or by genetic complementation with purB. Addition of adenine or genetic complementation also restored the invasion efficiency of the Nal r clone. This report reconciles longstanding inconsistencies in phenotypic properties of an archetypal strain and provides both reassurance and cautions regarding intentional and unintentional evolution in vitro.

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“…The first of these is FtsK. The cytoplasmic domain of this protein is involved in chromosome resolution and is not essential for cell division, whereas the transmembrane and periplasmic domains are essential but their only known function is in the recruitment of other division proteins (2,12,13). After a time delay, the FtsQ, FtsL, FtsB, FtsW, FtsI, and FtsN proteins are rapidly recruited (14).…”

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A New Essential Cell Division Protein in Caulobacter crescentus

et al. 2017

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Bacterial cell division is a complex process that relies on a multiprotein complex composed of a core of widely conserved and generally essential proteins and on accessory proteins that vary in number and identity in different bacteria. The assembly of this complex and, particularly, the initiation of constriction are regulated processes that have come under intensive study. In this work, we characterize the function of DipI, a protein conserved in Alphaproteobacteria and Betaproteobacteria that is essential in Caulobacter crescentus. Our results show that DipI is a periplasmic protein that is recruited late to the division site and that it is required for the initiation of constriction. The recruitment of the conserved cell division proteins is not affected by the absence of DipI, but localization of DipI to the division site occurs only after a mature divisome has formed. Yeast two-hybrid analysis showed that DipI strongly interacts with the FtsQLB complex, which has been recently implicated in regulating constriction initiation. A possible role of DipI in this process is discussed.IMPORTANCE Bacterial cell division is a complex process for which most bacterial cells assemble a multiprotein complex that consists of conserved proteins and of accessory proteins that differ among bacterial groups. In this work, we describe a new cell division protein (DipI) present only in a group of bacteria but essential in Caulobacter crescentus. Cells devoid of DipI cannot constrict. Although a mature divisome is required for DipI recruitment, DipI is not needed for recruiting other division proteins. These results, together with the interaction of DipI with a protein complex that has been suggested to regulate cell wall synthesis during division, suggest that DipI may be part of the regulatory mechanism that controls constriction initiation.KEYWORDS Caulobacter crescentus, SH3 domain, bacterial cell division, constriction initiation, divisome B acterial cell division is a complex process involving the action of a multiprotein complex known as the divisome (1, 2). In Escherichia coli, the divisome is composed of approximately 30 proteins that assemble into a complex spanning from the cytoplasm to the outer membrane (OM). Of these proteins, only 12 are essential in E. coli and 11 are widely conserved in other bacteria, suggesting that they constitute the core of the divisome (3, 4). The divisome complex starts assembling when a ring formed by the FtsZ protein is stabilized at the site where division will occur (5, 6). FtsZ is a tubulin-related cytoplasmic protein that is brought near the cytoplasmic membrane through its interactions with the membrane-associated protein FtsA and, in E. coli, the transmembrane protein ZipA (7,8). The FtsZ ring generates a force sufficient to deform lipid membranes and probably drives the constriction of the inner membrane (9, 10). After establishment of the FtsZ ring, the FtsEX complex is recruited through the interaction of FtsE with FtsZ (11). The divisome then expands to the peripla...

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TheEscherichia coliFtsK functional domains involved in its interaction with its divisome protein partners

Cited by 25 publications

References 17 publications

Site-directed Fluorescence Labeling Reveals a Revised N-terminal Membrane Topology and Functional Periplasmic Residues in the Escherichia coli Cell Division Protein FtsK

Site-directed Fluorescence Labeling Reveals a Revised N-terminal Membrane Topology and Functional Periplasmic Residues in the Escherichia coli Cell Division Protein FtsK

In Vitro Evolution of an Archetypal Enteropathogenic Escherichia coli Strain

A New Essential Cell Division Protein in Caulobacter crescentus

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