Only the N-Terminal Domain of FtsK Functions in Cell Division

Draper, G. Craig; McLennan, Neil; Begg, K J; Masters, Millicent; Donachie, W.

doi:10.1128/jb.180.17.4621-4627.1998

Cited by 131 publications

(99 citation statements)

References 26 publications

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“…pcI P22 or pcI 434 . phenotype of the mutant described in Draper et al (1998), could explain the discrepancy between our result and that described previously. As far as the FtsK fragment 725-1329 is concerned (Fig.…”

Section: Resultscontrasting

confidence: 99%

“…FtsK structural analysis showed that the protein consists of an N-terminal domain (about 200 residues) with several predicted membrane-spanning regions involved in cell division (Draper et al, 1998;Wang & Lutkenhaus, 1998;Yu et al, 1998), a proline-glutamine-rich domain (linker region of about 500 residues) and a C-terminal domain with a nucleotide-binding consensus sequence of about 500 amino acids involved in DNA segregation (Yu et al, 1998;Steiner et al, 1999;Bigot et al, 2004).…”

Section: Resultsmentioning

confidence: 99%

“…FtsK is a polytopic membrane protein that can be divided into three domains. The N-terminal domain (about 200 residues), involved in cell division (Draper et al, 1998;Wang & Lutkenhaus, 1998;Yu et al, 1998), contains four transmembrane helices (Dorazi & Dewar, 2000) and localizes to the septal ring, where it is necessary for the recruitment of other division proteins (Chen & Beckwith, 2001). The remainder of FtsK is cytoplasmic and consists of a long proline-and glutamine-rich linker region (about 500 amino acids), followed by the C-terminal domain (about 500 residues) involved in DNA segregation (Yu et al, 1998;Steiner et al, 1999;Bigot et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

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

Grenga

Luzi

Paolozzi

et al. 2008

FEMS Microbiology Letters

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FtsK is a multifunctional protein involved in both cell division and chromosome segregation. As far as its role in cell division is concerned, FtsK is among the first divisome proteins that localizes at mid-cell, after FtsZ, FtsA and ZipA, and is required for the recruitment of the other divisome components. The ability of FtsK to interact with several cell division proteins, namely FtsZ, FtsQ, FtsL and FtsI, by the two-hybrid assay was already shown by our group. In this work, we describe the identification of the protein domain(s) involved in the interaction with the cell division partner proteins. The biological role of some interactions is also discussed.

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Section: Resultscontrasting

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Grenga

Luzi

Paolozzi

et al. 2008

FEMS Microbiology Letters

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“…These observations are consistent with a defect in membrane fusion, but it has also been suggested that FtsK is needed for the final stages of peptidoglycan synthesis because FtsK deletions can be rescued by deleting dacA, which encodes a carboxypeptidase (Draper et al, 1998). FtsK deletions can also be suppressed by overexpression of FtsN (Draper et al, 1998), the structure of which has revealed a potential peptidoglycan binding site (Yang et al, 2004).…”

Section: The Z Ring Undergoes Rapid Turnoversupporting

confidence: 76%

“…While an ftsK depletion strain forms smooth filaments, indicating that FtsK is required to initiate cytokinesis, several point and truncation mutants form deep constrictions, as if these forms of FtsK are specifically defective in the final stages of septum closure (Begg et al, 1995;Diez et al, 1997;Wang and Lutkenhaus, 1998;Yu et al, 1998a). These observations are consistent with a defect in membrane fusion, but it has also been suggested that FtsK is needed for the final stages of peptidoglycan synthesis because FtsK deletions can be rescued by deleting dacA, which encodes a carboxypeptidase (Draper et al, 1998). FtsK deletions can also be suppressed by overexpression of FtsN (Draper et al, 1998), the structure of which has revealed a potential peptidoglycan binding site (Yang et al, 2004).…”

Section: The Z Ring Undergoes Rapid Turnovermentioning

confidence: 75%

Bacterial cell division and the septal ring

Weiss

2004

Molecular Microbiology

206

204

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Cell division in bacteria is mediated by the septal ring, a collection of about a dozen (known) proteins that localize to the division site, where they direct assembly of the division septum. The foundation of the sep-tal ring is a polymer of the tubulin-like protein FtsZ. Recently, experiments using fluorescence recovery after photobleaching have revealed that the Z ring is extremely dynamic. FtsZ subunits exchange in and out of the ring on a time scale of seconds even while the overall morphology of the ring appears static. These findings, together with in vitro studies of purified FtsZ, suggest that the rate-limiting step in turnover of FtsZ polymers is GTP hydrolysis. Another component of the septal ring, FtsK, is involved in coordinating chromosome segregation with cell division. Recent studies have revealed that FtsK is a DNA translocase that facilitates decatenation of sister chromosomes by TopIV and resolution of chromosome dimers by the XerCD recombinase. Finally, two murein hydrolases, AmiC and EnvC, have been shown to localize to the septal ring of Escherichia coli , where they play an important role in separation of daughter cells. Scope of this review This MicroReview opens with a whirlwind tour of cell division in Escherichia coli. To keep it short and to the point, I have made some oversimplifications and relied almost exclusively on citations to a collection of review articles rather than the original studies. The remainder of the review is devoted to a more detailed and critical look at a few questions that have been the focus of several recent studies. (i) How do the proteins that comprise the septal ring work together during cytokinesis? One step towards answering this question is to identify protein-protein interactions among the division proteins. I will summarize what is known about this topic and suggest reasons why progress has been slow. (ii) How does FtsZ drive cytoki-nesis? Although the answer remains elusive, recent experiments suggest the rate-limiting step in turnover of the FtsZ polymer is GTP hydrolysis. I will speculate on the implications that this has for the ability of FtsZ to generate force. (iii) How is septum assembly coordinated with partitioning of chromosomes to daughter cells? At least three mechanisms by which FtsK prevents the septum from closing on the chromosomes like a guillotine have been elucidated. I will describe these activities, and briefly compare FtsK with a similar protein, SpoIIIE, involved in sporulation in Bacillus subtilis. (iv) How are daughter cells separated? Two peptidoglycan hydrolases, AmiC and EnvC, have recently been shown to localize to the septal ring and play an important role in this process in E. coli.

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FtsK DNA Translocase: The Fast Motor That Knows Where It's Going

Crozat

Grainge

2010

ChemBioChem

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FtsK is a double-stranded DNA translocase, a motor that converts the chemical energy of binding and hydrolysing ATP into movement of a DNA substrate. It moves DNA at an amazing rate->5000 bp per second-and is powerful enough to remove other proteins from the DNA. In bacteria it is localised to the site of cell division, the septum, where it functions as a DNA pump at the late stages of the cell cycle, to expedite cytokinesis and chromosome segregation. The N terminus of the protein is involved in the cell-cycle-specific localisation and assembly of the cell-division machinery, whereas the C terminus forms the motor. The motor portion of FtsK has been studied by a combination of biochemistry, genetics, X-ray crystallography and single-molecule mechanical assays, and these will be the focus here. The motor can be divided into three subdomains: α, β and γ. The α and β domains multimerise to produce a hexameric ring with a central channel for dsDNA, and contain a RecA-like nucleotide-binding/hydrolysis fold. The motor is given directionality by the regulatory γ domain, which binds to polarised chromosomal sequences-5'-GGGNAGGG-3', known as KOPS-to ensure that the motor is loaded onto DNA in a specific orientation such that subsequent translocation is always towards the region of the chromosome where replication usually terminates (the terminus), and specifically to the 28 bp dif site, located in this region. Once the FtsK translocase has located the dif site it then interacts with the XerCD site-specific recombinases to activate recombination.

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Only the N-Terminal Domain of FtsK Functions in Cell Division

Cited by 131 publications

References 26 publications

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

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

Bacterial cell division and the septal ring

FtsK DNA Translocase: The Fast Motor That Knows Where It's Going

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