Regulation of cell division in Escherichia coli K-12: probable interactions among proteins FtsQ, FtsA, and FtsZ

Descoteaux, Abigail E.; Drapeau, Gabriel R.

doi:10.1128/jb.169.5.1938-1942.1987

Cited by 38 publications

(19 citation statements)

References 31 publications

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“…It has also been shown that increased gene dosage offtsI is detrimental to division inftsZ,ftsA , andftsQ mutants, suggesting a functional interaction between these proteins (17). Interactions between these proteins has been inferred from other studies as well (14). In addition, our recent immunolocalization studies showed that inactivation of either FtsA, FtsQ, or PBP3 affected FtsZ ring formation or its stability (8).…”

Section: Discussionmentioning

confidence: 99%

The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli

1992

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Interactions among cell division genes in Escherichia coli were investigated by examining the effect on cell division of increasing the expression of theftsZ,fts4, orftsQ genes. We determined that cell division was quite sensitive to the levels of FtsZ and FtsA but much less so to FtsQ. Inhibition of cell division due to an increase in FtsZ could be suppressed by an increase in FtsA. Inhibition of cell division due to increased FtsA could be suppressed by an increase in FtsZ. In addition, although wild-type strains were relatively insensitive to overexpression ofJftQ, we observed that cell division was sensitized toftsQ overexpression in ftsl,ftL4, andftsZ mutants. Among these, theftsI mutant was the most sensitive. These results suggest that these gene products may interact and that the proper ratio of FtsZ to FtsA is critical for cell division to occur.

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Section: Discussionmentioning

confidence: 99%

The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli

1992

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“…At too high a concentration of FtsZ, however, the structure of the complex might be modified with the consequence that its activity is reduced, and therefore septation is initiated less frequently. It has been shown that the presence of a multicopy plasmid harboring the wild-type ftsZ gene in a ftsQJ mutant or a wild-type ftsQ gene in GD113 cells is more detrimental to cell growth and/or cell division than when the same plasmids are present in the wild-type cells (3). This suggests that an increase in the level of one of the Fts proteins in a cell which contains a mutationally alterated Fts protein can more drastically affect the distribution of the protein molecules within the complex.…”

Section: Sp Ebmentioning

confidence: 99%

“…To ensure that this inhibition was not due to an increased production of FtsZ without the presence of FtsQ and FtsA, we included wild-type copies offtsQ and ftsA in all of the plasmids that we tested. The inclusion of these genes was considered to be important because the Fts proteins probably form a functional complex, and any discrepancy in the concentration ratios of these proteins may have a deleterious effect on the formation and hence on the activity of such a complex (3).…”

Section: Sp Ebmentioning

confidence: 99%

Cell division control in Escherichia coli K-12: some properties of the ftsZ84 mutation and suppression of this mutation by the product of a newly identified gene

Phoenix

Drapeau

1988

J Bacteriol

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The Fts proteins play an important role in the control of cell division in Escherichia coli. These proteins, which possibly form a functional complex, are encoded by genes that form an operon. In this study, we examined the properties of the temperature-sensitive mutationftsZ84 harbored by low-or high-copy-number plasmids. Cells of strain AB1157, which had the ftsZ84 mutation, did not form colonies on salt-free L agar at 30°C. When a low-copy-number plasmid containing the ftsZ84 mutation was present in these mutant cells, colony formation was restored on this medium at 30°C, suggesting that FtsZ84 is probably less active than the wild-type protein and is therefore limiting in its capacity to trigger cell divisions. On the other hand, when the ftsZ84 mutation was harbored by the high-copy-number plasmid pBR325, colony formation was prevented on salt-free L agar plates whether the recipients were ftsZ84 mutant or parental cells, suggesting that, at high levels, FtsZ84 acts as a division inhibitor. The fact that colony formation was also prevented at 42°C indicates that the FtsZ84 protein is not inactivated at the nonpermissive temperature. The possibility that FtsZ84 is a more efficient division inhibitor than the wild-type FtsZ is discussed. Evidence is also presented showing that a gene adjacent to mutT codes for a product that, under certain conditions, suppresses the ftsZ84 mutation.

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“…It has been proposed that FtsA is a component of a membrane-associated complex (septator or divisome), which would include periplasmic, transmembrane, and cytoplasmic proteins acting coordinately to perform septation (27,35). Genetic analysis suggests that FtsA may interact, directly or indirectly, with other cell division proteins, such as FtsZ, PBP3, FtsQ, and FtsN (9,10,24,33,34). The FtsZ/FtsA ratio is important for cell division, and the localization of FtsA to a central position along the cell length depends on the formation of the FtsZ ring (1,8,11,15,23).…”

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Role of the Carboxy Terminus of Escherichia coli FtsA in Self-Interaction and Cell Division

et al. 2000

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The role of the carboxy terminus of the Escherichia coli cell division protein FtsA in bacterial division has been studied by making a series of short sequential deletions spanning from residue 394 to 420. Deletions as short as 5 residues destroy the biological function of the protein. Residue W415 is essential for the localization of the protein into septal rings. Overexpression of the ftsA alleles harboring these deletions caused a coiled cell phenotype previously described for another carboxy-terminal mutation (Gayda et al., J. Bacteriol. 174:5362-5370, 1992), suggesting that an interaction of FtsA with itself might play a role in its function. The existence of such an interaction was demonstrated using the yeast two-hybrid system and a protein overlay assay. Even these short deletions are sufficient for impairing the interaction of the truncated FtsA forms with the wild-type protein in the yeast two-hybrid system. The existence of additional interactions between FtsA molecules, involving other domains, can be postulated from the interaction properties shown by the FtsA deletion mutant forms, because although unable to interact with the wild-type and with FtsA⌬1, they can interact with themselves and cross-interact with each other. The secondary structures of an extensive deletion, FtsA⌬27, and the wild-type protein are indistinguishable when analyzed by Fourier transform infrared spectroscopy, and moreover, FtsA⌬27 retains the ability to bind ATP. These results indicate that deletion of the carboxy-terminal 27 residues does not alter substantially the structure of the protein and suggest that the loss of biological function of the carboxy-terminal deletion mutants might be related to the modification of their interacting properties.FtsA is an essential cell division protein of Escherichia coli that is widely conserved in bacteria. Together with ftsZ, which codes for a GTPase analog of the eukaryotic tubulin, ftsA forms one of the most frequently conserved gene pairs among the cell division genes in the eubacteria. Based on sequence homology it has been proposed that FtsA belongs to the sugar kinase/hsp70/actin superfamily (4). This superfamily comprises several proteins with a common two-domain topology and the ability to bind and hydrolyze ATP. FtsA binds to columns of ATP-agarose and can be isolated from cells either as a phosphorylated or a nonphosphorylated form (29), but so far no other biochemical function has been described for this protein.FtsA is present both in the cytoplasm and in the cytoplasmic membrane (29), where it forms a structural part of the septum (32). It has been proposed that FtsA is a component of a membrane-associated complex (septator or divisome), which would include periplasmic, transmembrane, and cytoplasmic proteins acting coordinately to perform septation (27,35). Genetic analysis suggests that FtsA may interact, directly or indirectly, with other cell division proteins, such as FtsZ, PBP3, FtsQ, and FtsN (9,10,24,33,34). The FtsZ/FtsA ratio is important for cell division, an...

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Regulation of cell division in Escherichia coli K-12: probable interactions among proteins FtsQ, FtsA, and FtsZ

Cited by 38 publications

References 31 publications

The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli

The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli

Cell division control in Escherichia coli K-12: some properties of the ftsZ84 mutation and suppression of this mutation by the product of a newly identified gene

Role of the Carboxy Terminus of Escherichia coli FtsA in Self-Interaction and Cell Division

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