Previous Article | Next Article 
Journal of Bacteriology, February 2000, p. 613-619, Vol. 182, No. 3
Department of Microbiology, University of
Connecticut Health Center, Farmington, Connecticut 06032
Received 26 April 1999/Accepted 3 November 1999
Escherichia coli cells contain potential division sites
at midcell and adjacent to the cell poles. Selection of the correct division site at midcell is controlled by three proteins: MinC, MinD,
and MinE. It has previously been shown (D. Raskin and P. de Boer, Cell
91:685-694, 1997) that MinE-Gfp localizes to the midcell site in an
MinD-dependent manner. We use here Gfp-MinD to show that MinD
associates with the membrane around the entire periphery of the cell in
the absence of the other Min proteins and that MinE is capable of
altering the membrane distribution pattern of Gfp-MinD. Studies with
the isolated N-terminal and C-terminal MinE domains indicated different
roles for the two MinE domains in the redistribution of
membrane-associated MinD.
Cell division in Escherichia
coli and most other rod-shaped bacteria occurs by formation of a
division septum at the midpoint of the cell, thus ensuring the
equipartition of cytoplasmic components into the two daughter cells. To
ensure that division occurs only at the midcell site, the cell must
select this site in preference to other potential division sites that
are located adjacent to the cell poles. If the polar sites are used to
support septum formation, small chromosomeless minicells are formed
that are incapable of undergoing further divisions. In E. coli, the selective suppression of the polar division sites is
accomplished by the cooperative action of the three gene products of
the minCDE locus: MinC, MinD, and MinE.
Previous studies (4) have shown that the three Min proteins
act in the following way. MinC and MinD act in concert to form a
nonspecific inhibitor of septation. In this process, MinD functions to
activate the latent division inhibitory activity of MinC
(6). The MinCD division inhibitor lacks site specificity, as
shown by the observation that expression of minC and
minD in the absence of minE leads to a block in
septation at all potential division sites, leading to formation of long
nonseptate filaments. Filamentation is suppressed by MinE, which acts
as a topological specificity factor to prevent the division inhibitor
from acting at the midcell site while permitting it to block septation
at polar division sites.
The ability of MinE to counteract the MinCD division inhibitor and the
ability to impart topological specificity to the system reside in
different domains of the 88-amino-acid MinE protein. The N-terminal
MinE domain is responsible for the anti-MinCD function, as shown by the
ability of MinE1-22 (20) or
MinE1-34 (13) to prevent MinCD-induced
filamentation. (Superscripts [e.g., minE1-53]
refer to amino acid positions within MinE or within the minE gene product.) The C-terminal domain of MinE is thought to encode the
MinE topological specificity function that is responsible for limiting
its action to the division site at midcell. It has been proposed that
topological specificity is accomplished by the binding of the
C-terminal topological specificity domain to a putative topological
target molecule at the new division site at midcell (17).
The sequestration of MinE at midcell would permit it to interfere with
the division inhibitor at this site without interfering with the
division inhibition activity at the unwanted polar division sites. As a
result, normal cell division would occur and polar divisions would be
prevented. Excess MinE has been shown to induce minicell formation,
suggesting that once the topological target is saturated, the excess
MinE molecules are free to counteract the division inhibitor elsewhere
in the cell.
Consistent with the ability of MinE to specifically counteract the
division inhibitor at midcell, a MinE-green fluorescent protein chimera
(MinE-Gfp) localizes to a ring-like structure at sites adjacent to the
midcell, and this localization pattern requires the simultaneous
expression of minD (14). This implicates MinD in
the process that leads to localization of MinE at midcell.
MinD plays several roles in the Min system. First, it activates the
MinC division inhibitor. Second, it is required to make the division
inhibitor sensitive to MinE (5, 10). Third, MinD is required
to localize MinE at midcell (14). After the initial
submission of the present study for publication, it was shown in a
related study that MinD localizes to the cell pole in a MinE-dependent
fashion and undergoes a rapid oscillation from pole to pole
(16).
We have also examined the cellular localization of the MinD protein and
its membrane interactions with MinE by using a green fluorescent
protein-MinD fusion protein (Gfp-MinD) to monitor the cellular
distribution of MinD. In this report we describe the membrane
rearrangements of Gfp-MinD that are induced by coexpression with MinE,
and we define a specific role for the N-terminal MinE domain in this process.
Bacterial strains.
E. coli PB114 ( Plasmids.
pSY1057
(Plac-minE22-88), a pUC derivative,
has been previously described (19). pJPB262
(Plac-minE1-32) was a gift from
Jean-Pierre Bouché (13); this pUC8-derived plasmid
contains a termination codon immediately after
minE1-32 and the
minE33-88 portion of minE has been deleted.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Membrane Redistribution of the Escherichia
coli MinD Protein Induced by MinE
ABSTRACT
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
INTRODUCTION
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
MATERIALS AND METHODS
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
DB217) was
derived from PB114 (
minCDE) (4) and DB217
(Plac-minC). DB217 was constructed by in vivo
recombination of plasmid pDB217 (6) with NT5
(3). E. coli RC1 [minCDE (araAB01C-leu)] was constructed by P1-mediated
transduction of min from PB114 into E. coli MC1000.
Growth conditions.
Strains were grown overnight on L agar
plates containing 1% glucose and antibiotics needed for plasmid
maintenance (50 or 100 µg of ampicillin per ml for pUC or
pBluescript-derived plasmids and 20 µg of chloramphenicol per ml for
pBAD33-derived plasmids) and were inoculated the next morning into L
broth containing the same additives. After 3 to 4 h of growth at
37°C, the cells were collected by centrifugation, washed twice with L
broth, and suspended at an A600 of 0.04 in fresh
L broth lacking glucose but containing antibiotics and inducer, where
indicated. Unless otherwise stated, genes under
Para control were expressed by growth in 0.001 to 0.005% arabinose, while genes under Plac
control were expressed at basal levels by growth in the absence of IPTG
(isopropyl-
-D-thiogalactopyranoside). The cultures were
incubated with shaking at 30°C for 4 to 4.5 h, and cells were
sampled directly from the culture for microscopy (unfixed) or were
fixed by addition to the culture of 1.7% formaldehyde and 0.17%
glutaraldehyde (final concentrations), followed by incubation at room
temperature for 45 min. The fixed cells were collected by
centrifugation, resuspended in 0.9% saline, and stored at 4°C until
microscopic examination. Western blot analysis showed that the
concentrations of Gfp-MinD in minCDE cells containing
plasmid pSLR22
(Para-gfp::minD), in cells
grown for 4.5 h in the presence of 0.001 or 0.0025% arabinose,
were 0.96- and 1.78-fold the concentration of MinD in the wild-type
strain, respectively. In minCDE cells containing plasmid
pSLR23 (Para-gfp::minD
minE) and grown in the presence of 0.001 or 0.0025% arabinose,
the concentrations of Gfp-MinD were 1.17- and 2.1-fold and the
concentrations of MinE were 5.0- and 9.5-fold, respectively, their
concentrations in the wild-type strain.
Gel electrophoresis and immunoblotting. Cells for Western blot analysis were harvested by centrifugation and frozen immediately. Frozen samples were thawed by resuspension in sodium dodecyl sulfate-polyacrylamide gel electrophoresis loading buffer, boiled for 5 min, and subjected to sodium dodecyl sulfate-gel electrophoresis (11). Immunoblots were performed as previously described by using antibodies directed against MinE2-19 to compare the concentrations of MinE and N-terminal MinE fragments and antibody directed against a mixture of MinE29-38 and MinE70-88 to detect MinE+ or to compare the concentrations of MinE and of MinE C-terminal fragments (19, 20). Antibody raised against whole wild-type MinD protein was used to detect MinD and Gfp-MinD. Bands in Western blots were quantitated by using the ImageQuant program (Molecular Dynamics) on digitized images by using concentrations of cell extracts where the band intensity was proportional to amount of the sample applied to the gel.
Microscopy and data analysis. Samples were examined by phase contrast, Nomarski, and fluorescence microscopy. A minicell phenotype was defined by the presence of moderate to large numbers of spherical minicells, polar septa, and cells with a length ranging from the wild-type length to short filaments of approximately four to six cell lengths. A filamenting phenotype was defined by the virtual to complete absence of minicells and by the presence of large numbers of filaments, ranging from 6 to 100 cell lengths. Fluorescence images were collected by using an integrating charge-coupled device camera. Measurements of cell lengths and positions of cell landmarks and data analysis were done by using the public domain NIH Image program (http://rsb.info.nih.gov/nih-image/) and in-house software.
| |
RESULTS |
|---|
|
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
|
|---|
Phenotypic effects of a Gfp-MinD fusion protein. To study the cellular localization of MinD, we constructed a gfp::minD fusion that codes for a protein (Gfp-MinD) in which the high quantum yield Gfpmut2 (1) (called Gfp in the remainder of this study) is fused to the N-terminal end of MinD. The gfp::minD fusion was expressed under control of the arabinose-inducible BAD promoter to permit coexpression of other relevant genes under Plac control in the same cell.
MinD normally performs two functions that affect formation of the division septum and that can be assayed in vivo: (i) MinD is an activator of the MinC division inhibitor and (ii) MinD makes the division inhibitor sensitive to suppression by MinE. Evidence that the Gfp-MinD fusion protein retained these two functions was obtained by comparing the effects of MinD and Gfp-MinD on the division pattern of amin strain in the presence of MinC and/or MinE.
As previously reported (4), induction of minC
from an integrated Plac-minC prophage in the
absence of MinD failed to block division in a minCDE
strain (Fig. 1a), whereas coexpression of minC and minD led to the formation of nonseptate
filaments (Fig. 1b and c). Coexpression of minC and
gfp::minD also induced filamentation when Plac-minC and
Para-gfp::minD were
coinduced by growth in the presence of IPTG and arabinose (Fig. 1d). We
conclude that Gfp-MinD retained the MinC activation effect of MinD.
|
/pFX1
(minC+D+E+/Plac-minE1-53::gfp)
was grown for 4 h at 30° in L broth containing 0.05 mM IPTG (h)
or 1 mM IPTG (i). Bars, 5 µm.
prophage. As previously
described, the expression of minE suppressed the
filamentation that occurred when minC and minD
were coexpressed in the absence of minE (Fig. 1e).
Similarly, filamentation was suppressed when minD was
replaced by gfp::minD (in pSLR23, Fig. 1f). Thus, Gfp-MinD behaves similarly to MinD in making the activated MinC division inhibitor sensitive to MinE.
Raskin and de Boer (16) have shown that Gfp-MinD can correct
the minicelling phenotype of a minD1 mutant, in which the
mutation is located near the carboxy terminus of MinD (10).
This showed that the Gfp-MinD protein retains the MinD function that is
lost due to the minD1 mutation. In the present study,
evidence that Gfp-MinD could provide all of the functions of MinD was
obtained by expressing minC,
gfp::minD, and minE in
a minCDE strain (from PB114/pYW3
[minCDE/Plac-minC
gfp::minD minE]). As illustrated in Fig. 1g,
low-level derepression of Plac by growth of
PB114/pYW3 in 0.005% or 0% glucose or 10 µM IPTG led to almost
complete disappearance of the minicell phenotype. Similar results were
obtained with wild-type MinD, expressed from pDB170
(Plac-minC minD minE) (data not shown)
(4). In this case, minicelling was corrected at even lower
levels of derepression, obtained by growth in 0.05 or 0.01% glucose.
We conclude that Gfp-MinD has retained all of the important functions
of MinD, although the Gfp moiety may interfere somewhat with MinD
efficiency or stability.
Pattern of membrane-associated Gfp-MinD in the absence of
MinE.
It has previously been shown that MinE-Gfp can localize to
sites near midcell and that this localization requires the presence of
the MinD protein (14). We therefore studied the localization pattern of Gfp-MinD in the presence or absence of MinE. Experiments were performed in the min strain PB114. Because of the
min background, the cells showed a minicell phenotype
consisting of minicells plus cells ranging from wild-type cell length
to short filaments. Cells were examined after low-level induction of
Gfp-MinD from Para-gfp::minD by growth in
the presence of 0.001 to 0.005% arabinose. Under these conditions the
phenotype of the min host was unchanged.
|
Effect of MinE on the Gfp-MinD distribution pattern: polar
zones.
Evidence that MinE can induce changes in the distribution
pattern of membrane-associated MinD came from experiments in which gfp::minD was coexpressed with
minE in a min strain (RC1/pSLR22/pDB188 [min/Para-gfp::minD/Plac-minE])
by growth in the presence of 0.001 to 0.005% arabinose. Under these
conditions many cells in the population contained a long fluorescent
zone at one end of the cell (Fig. 3). In
unfixed cells, the polar zones of Gfp-MinD oscillated from pole-to-pole
(Fig. 4) as has previously been described (16).
|
|
Effect of MinE domains on localization of Gfp-MinD. Previous work has indicated that the topological specificity domain of MinE is located within the C-terminal region (MinE36-88) of the 88-amino-acid MinE protein and that the anti-MinCD domain that is capable of suppressing the action of the MinCD division inhibitor is located in the N-terminal region of the protein (MinE1-22 or MinE1-34) (13, 20). It has been suggested that the topological specificity domain interacts with a topological target at midcell to direct MinE localization at midcell, whereas the anti-MinCD domain of MinE is thought to interact with the MinCD system via MinD (17).
We therefore asked whether the ability of MinE to cause Gfp-MinD to coalesce into an extended membrane-associated structure at the cell pole required both of the MinE domains. In these experiments gfp::minD was expressed in amin host from pSLR22
(Para-gfp::minD) and
C-terminal or N-terminal MinE fragments were expressed under Plac control.
Coexpression of Gfp-MinD with a MinE fragment that contained the
topological specificity domain but lacked the anti-MinCD domain
(fragment MinE22-88, in pSY1057) did not significantly
alter the pattern that was present in the absence of MinE (Fig.
5c). Fluorescence was predominantly peripheral along the length of the cell, and no localized fluorescent zones were observed. Western blots with antibody directed against the
C-terminal region of MinE showed that the concentration of MinE22-88 was severalfold higher than the concentration of
full-length MinE (MinE1-88) in the experiments in which
Plac-minE1-88 was coexpressed with
gfp::minD (data not shown). Therefore,
the failure of the C-terminal MinE domain to affect the Gfp-MinD
pattern was not due to a lower cellular concentration of the fragment compared with the concentration of MinE1-88 in the
parallel experiments.
|
5.0-µm cell length), the zones were always located
at one end of the cell. In some longer cells, fluorescent zones were
present at both poles and were sometimes also present elsewhere along
the length of the cell. The polar fluorescence was predominantly
peripheral, indicating that it represented membrane-associated
Gfp-MinD. Strikingly, whenever polar zones were present, the remainder
of the cell periphery was essentially nonfluorescent (Fig. 5a, b, and
d). This was in sharp contrast to cells that expressed Gfp-MinD in the
absence of MinE, where the fluorescence was distributed around the
entire cell periphery. This implies that the MinE fragments were
responsible for the recruitment of essentially all of the
membrane-associated Gfp-MinD into the polar zones.
Studies of unfixed cells showed that the N-terminal portion of MinE
induced both the segregation of Gfp-MinD to one pole and its subsequent
back-and-forth movement to the opposite pole (Fig. 6). The relatively slow oscillation may
reflect lower-than-optimal ratios of MinE to MinD, which can
significantly affect the rate of oscillation (16). The
presence of oscillatory pole-to-pole movement of Gfp-MinD in the
presence of MinE1-53 indicates that the mechanisms for the
MinE-dependent polar localization and for transpolar movement
of MinD do not require the topological specificity domain of MinE.
|
Localization of MinE-Gfp and MinE1-53-Gfp in the presence of MinD. Full-length MinE (as MinE-Gfp) forms a ring at midcell when expressed in the presence of MinD (14). This led to the suggestion that the midcell MinE ring might be responsible for sequestering Gfp-MinD to one of the ends of the cell to form the polar MinD zones and might also play a role in inducing disassembly of Gfp-MinD from the polar membrane binding site and subsequent pole-to-pole movement (16).
It has been previously shown that MinE1-33-Gfp fails to form midcell MinE rings (14) although, as shown in the present work, MinE1-32 was capable of inducing formation of polar zones of MinD-Gfp. Because MinE1-53 also induced the formation of polar MinD zones, we used MinE1-53-Gfp to determine whether MinE1-53 was capable of forming a MinE ring at midcell. Localization studies in cells where MinE1-53-Gfp was coexpressed with MinD failed to show the characteristic MinE rings that are seen with full-length MinE-Gfp (Fig. 7). This confirms that the N-terminal MinE domain is unable to localize at midcell in the absence of the C-terminal topological specificity domain, although it is capable of inducing the redistribution of MinD into polar zones. These results suggest that a MinE ring is not required for the formation of polar zones of MinD.
|
| |
DISCUSSION |
|---|
|
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
|
|---|
Proper placement of the E. coli division septum requires that MinD and MinE function cooperatively to modulate the division potential of cellular sites that are located at midcell and at the cell poles. A MinD-MinE interaction in this process is implied by the fact that localization of MinE at midcell requires MinD, that MinD is required to make the MinC division inhibitor sensitive to suppression by MinE, and that MinE is required for the formation of MinD zones at the cell pole.
Gfp-MinD is capable of associating with the membrane around the entire periphery of the cell in the absence of MinE and MinC, as shown by Raskin and de Boer (16) and as confirmed in the present study. In contrast, the membrane association of MinE (14) and MinC (9, 15) both require the presence of MinD. These observations suggest that the membrane attachment of MinD is the initial step in the membrane assembly of the Min proteins. The MinD sequence does not include an apparent membrane-spanning domain, and cell fractionation and immunoelectronmicroscopic studies suggest that MinD is a peripheral membrane protein (2). This suggests that MinD is likely to interact with another membrane component that anchors it to the membrane surface.
MinE dramatically changes the membrane distribution of MinD so that essentially all of the membrane-associated Gfp-MinD is recruited into a broad zone at one cell pole (reference 16 and this study). Previous studies with Gfp-MinE (14) have shown that MinE forms a ring near midcell under the same conditions that lead to formation of the polar zones of MinD, raising the possibility (16) that the midcell MinE ring plays a role in the observed redistribution of membrane-associated MinD. The present observations suggest that the two events, i.e., the formation of the midcell MinE ring and the formation of polar zones of MinD, are unrelated phenomena. Thus, in the present study the N-terminal domain of MinE, which did not form a midcell MinE ring in studies of MinE1-53-Gfp (this study) and MinE1-33-Gfp (14), was capable of inducing formation of polar zones of Gfp-MinD with high efficiency. This argues against models in which the MinE ring at midcell acts as a gasket to sequester Gfp-MinD to one end of the cell and/or to provoke release of Gfp-MinD from one pole so that it can move to the opposite pole (16).
Because MinE1-53 and MinE1-34 fragments retain their ability to counteract the division-inhibitory action of MinCD in a MinD-dependent fashion (13, 20), it is likely that the N-terminal MinE domain is the domain that interacts with MinD. It is this interaction that presumably provokes the redistribution of membrane-associated MinD to the cell pole.
We suggest the following sequence of events to explain the cooperative actions of MinE and MinD, based on the idea that formation of the MinE ring at midcell and formation of the MinD zone at the cell pole both result from the lateral movement of MinD within the two-dimensional membrane matrix. First, MinD associates with the inner surface of the cytoplasmic membrane around the entire periphery of the cell. Second, the N-terminal domain of MinE interacts with the membrane-associated MinD. This recruits MinE to the membrane. We speculate that the MinD-MinE interaction may alter MinD or its membrane attachment to permit MinD molecules to diffuse laterally within the two-dimensional membrane matrix, possibly in association with its putative membrane anchor. Alternatively, MinD may always be laterally mobile within the membrane. In this case, MinE could modify MinD to increase its affinity for polar sites (discussed below). This alternative is perhaps less likely since the fact that Gfp-MinD forms polar arcs in the absence of MinE (Fig. 2a) implies that MinD has affinity for the cell pole independently of MinE. In either case, the laterally mobile MinD molecules are suggested to be responsible both for the formation of the MinE ring at midcell and for the formation of the MinD polar zones. Third, when the laterally mobile MinD-MinE complex encounters the putative topological target for MinE at midcell, the midcell target interacts with the C-terminal topological specificity domain of MinE, thereby anchoring MinE as a ring structure at midcell and releasing it from its MinD carrier. This finding is consistent with the observation that the topological specificity domain is required for formation of the midcell MinE ring. Fourth, unrelated to formation of the MinE ring, the collision of laterally mobile MinD molecules with a hypothetical membrane-associated nucleation site adjacent to a cell pole leads to formation of a side-by-side array of MinD molecules (the polar zone) whose assembly depends on collisional interactions within the membrane matrix. The two-dimensional MinD lattice would be expected to grow and coalesce until most or all of the mobile membrane-associated MinD molecules were captured by collision with the polar lattice. This would explain the striking observation that only a single Gfp-MinD zone was present in most cells, with no visible fluorescence elsewhere in the membrane.
The fact that the MinD zone is apparently formed at only one pole might reflect a rapid MinD assembly process following the initial interaction with one of the polar nucleation sites, a process similar to the cooperative assembly process suggested by Raskin and de Boer (16). The forces that capture and retain MinD molecules within the polar zone have yet to be defined. The lattice could be based on direct interactions between MinD molecules or could involve the noncovalent cross-linking of MinD molecules or oligomers by another component that would also be part of the polar lattice structure. The suggested model invokes lateral diffusion of MinD molecules as the key event in the formation of the MinD polar zones and in the MinD-facilitated formation of the midcell MinE ring. The possibility also exists that the lateral translocation event might in part be an active process in which MinE modifies MinD into a form that can be actively translocated along the membrane.
A precedent for the capture of mobile membrane molecules into a single structure exists in the well-established ability of antibody molecules or lectins to induce the redistribution of eucaryotic membrane-associated surface proteins by noncovalently crosslinking them into "patches" and "caps" that are reminiscent of the Gfp-MinD structures described here (7, 12, 18). Ultimately, all of the proteins are captured into a single large domain, one analogous to the Gfp-MinD zones that are formed at the cell pole.
In an entirely different type of model, MinD would move directly from the cytoplasm to the polar membrane sites after its interaction with MinE. This cannot be excluded although it would require a second mechanism to explain the requirement for MinD in formation of the midcell MinE ring. Further work will be needed to distinguish between these and other possible models.
| |
ACKNOWLEDGMENTS |
|---|
This work was supported by grants from the National Institutes of Health to L.I.R. (GM41978 and GM53276). S.L.R. was a Long Term Fellow of the Human Frontiers Science Program.
| |
FOOTNOTES |
|---|
* Corresponding author. Mailing address: Department of Microbiology, University of Connecticut Health Center, Farmington, CT 06032. Phone: (860) 679-3581. Fax: (860) 679-1239. E-mail: lroth{at}panda.uchc.edu.
Present address: Department of Biochemistry, UMDNJ-Robert Wood
Johnson Medical School, Piscataway, NJ 08854.
| |
REFERENCES |
|---|
|
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
|
|---|
| 1. | Cormack, B. P., R. H. Valdivia, and S. Falkow. 1996. FACS-optimised mutants of the green fluorescent protein (GFP). Gene 173:33-38[CrossRef][Medline]. |
| 2. | de Boer, P. A. J., R. E. Crossley, A. R. Hand, and L. I. Rothfield. 1991. The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site. EMBO J. 10:4371-4380[Medline]. |
| 3. |
de Boer, P. A. J.,
R. E. Crossley, and L. I. Rothfield.
1988.
Isolation and properties of minB, a complex genetic locus involved in correct placement of the division site in Escherichia coli.
J. Bacteriol.
170:2106-2112 |
| 4. | de Boer, P. A. J., R. E. Crossley, and L. I. Rothfield. 1989. A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli. Cell 56:641-649[CrossRef][Medline]. |
| 5. |
de Boer, P. A. J.,
R. E. Crossley, and L. I. Rothfield.
1990.
Central role for the Escherichia coli minC gene product in two different cell division-inhibition systems.
Proc. Natl. Acad. Sci. USA
87:1129-1133 |
| 6. |
de Boer, P. A. J.,
R. E. Crossley, and L. I. Rothfield.
1992.
Roles of MinC and MinD in the site-specific septation block mediated by the MinCDE system of Escherichia coli.
J. Bacteriol.
174:63-70 |
| 7. | Edelman, G. 1976. Some new views of the cell surface. J. Biochem. 79:1P-12P. |
| 8. |
Guzman, L.,
D. Belin,
M. J. Carson, and J. Beckwith.
1995.
Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter.
J. Bacteriol.
177:4121-4130 |
| 9. | Hu, Z., and J. Lutkenhaus. 1999. Topological regulation in Escherichia coli involves rapid pole-to-pole oscillation of the division inhibitor MinC under the control of MinD and MinE. Mol. Microbiol. 34:82-90[CrossRef][Medline]. |
| 10. |
Labie, C.,
F. Bouché, and J.-P. Bouché.
1990.
Minicell-forming mutants of Escherichia coli: suppression of both DicB- and MinD-dependent division inhibition by inactivation of the minC gene product.
J. Bacteriol.
172:5852-5855 |
| 11. | Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685[CrossRef][Medline]. |
| 12. | Nicolson, G. 1974. The interactions of lectins with animal cell surfaces. Int. Rev. Cytol. 39:89-190[Medline]. |
| 13. | Pichoff, S., B. Vollrath, C. Touriol, and J.-P. Bouché. 1995. Deletion analysis of gene minE which encodes the topological specificity factor of cell division in Escherichia coli. Mol. Microbiol. 18:321-329[CrossRef][Medline]. |
| 14. | Raskin, D., and P. de Boer. 1997. The MinE ring: an FtsZ-independent cell structure required for selection of the correct division site in E. coli. Cell 91:685-694[CrossRef][Medline]. |
| 15. |
Raskin, D., and P. de Boer.
1999.
MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli.
J. Bacteriol.
181:6419-6424 |
| 16. |
Raskin, D., and P. de Boer.
1999.
Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli.
Proc. Natl. Acad. Sci. USA
96:4971-4976 |
| 17. | Rothfield, L. I., and C.-R. Zhao. 1996. How do bacteria decide where to divide? Cell 84:183-186[CrossRef][Medline]. |
| 18. | Taylor, R. B., W. P. H. Duffus, M. C. Raff, and S. de Petris. 1971. Redistribution and pinocytosis of lymphocyte surface immunoglobulin molecules induced by anti-immunoglobulin antibody. Nat. New Biol. 233:225-229. |
| 19. | Zhang, Y., S. Rowland, G. King, and L. Rothfield. 1998. Relation of the oligomeric structure of MinE to its topological specificity function. Mol. Microbiol. 30:265-273[CrossRef][Medline]. |
| 20. |
Zhao, C.-R.,
P. de Boer, and L. Rothfield.
1995.
Proper placement of the E. coli division site requires two functions that are associated with different domains of the MinE protein.
Proc. Natl. Acad. Sci. USA
92:4313-4317 |
Journal of Bacteriology, February 2000, p. 613-619, Vol. 182, No. 3
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
This article has been cited by other articles:
-
Varma, A., Huang, K. C., Young, K. D.
(2008). The Min System as a General Cell Geometry Detection Mechanism: Branch Lengths in Y-Shaped Escherichia coli Cells Affect Min Oscillation Patterns and Division Dynamics. J. Bacteriol.
190: 2106-2117
[Abstract] [Full Text] -
Shih, Y.-L., Rothfield, L.
(2006). The Bacterial Cytoskeleton. Microbiol. Mol. Biol. Rev.
70: 729-754
[Abstract] [Full Text] -
Taghbalout, A., Ma, L., Rothfield, L.
(2006). Role Of MinD-Membrane Association in Min Protein Interactions.. J. Bacteriol.
188: 2993-3001
[Abstract] [Full Text] -
Drew, D. A., Osborn, M. J., Rothfield, L. I.
(2005). A polymerization-depolymerization model that accurately generates the self-sustained oscillatory system involved in bacterial division site placement. Proc. Natl. Acad. Sci. USA
102: 6114-6118
[Abstract] [Full Text] -
Szeto, J., Acharya, S., Eng, N. F., Dillon, J.-A. R.
(2004). The N Terminus of MinD Contains Determinants Which Affect Its Dynamic Localization and Enzymatic Activity. J. Bacteriol.
186: 7175-7185
[Abstract] [Full Text] -
Johnson, J. E., Lackner, L. L., Hale, C. A., de Boer, P. A. J.
(2004). ZipA Is Required for Targeting of DMinC/DicB, but Not DMinC/MinD, Complexes to Septal Ring Assemblies in Escherichia coli. J. Bacteriol.
186: 2418-2429
[Abstract] [Full Text] -
Huang, K. C., Meir, Y., Wingreen, N. S.
(2003). Dynamic structures in Escherichia coli: Spontaneous formation of MinE rings and MinD polar zones. Proc. Natl. Acad. Sci. USA
100: 12724-12728
[Abstract] [Full Text] -
Szeto, T. H., Rowland, S. L., Habrukowich, C. L., King, G. F.
(2003). The MinD Membrane Targeting Sequence Is a Transplantable Lipid-binding Helix. J. Biol. Chem.
278: 40050-40056
[Abstract] [Full Text] -
Ma, L.-Y., King, G., Rothfield, L.
(2003). Mapping the MinE Site Involved in Interaction with the MinD Division Site Selection Protein of Escherichia coli. J. Bacteriol.
185: 4948-4955
[Abstract] [Full Text] -
Shih, Y.-L., Le, T., Rothfield, L.
(2003). Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles. Proc. Natl. Acad. Sci. USA
100: 7865-7870
[Abstract] [Full Text] -
Lackner, L. L., Raskin, D. M., de Boer, P. A. J.
(2003). ATP-Dependent Interactions between Escherichia coli Min Proteins and the Phospholipid Membrane In Vitro. J. Bacteriol.
185: 735-749
[Abstract] [Full Text] -
Suefuji, K., Valluzzi, R., RayChaudhuri, D.
(2002). Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE. Proc. Natl. Acad. Sci. USA
99: 16776-16781
[Abstract] [Full Text] -
Szeto, T. H., Rowland, S. L., Rothfield, L. I., King, G. F.
(2002). Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts. Proc. Natl. Acad. Sci. USA
99: 15693-15698
[Abstract] [Full Text] -
Gueiros-Filho, F. J., Losick, R.
(2002). A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ. Genes Dev.
16: 2544-2556
[Abstract] [Full Text] -
Johnson, J. E., Lackner, L. L., de Boer, P. A. J.
(2002). Targeting of DMinC/MinD and DMinC/DicB Complexes to Septal Rings in Escherichia coli Suggests a Multistep Mechanism for MinC-Mediated Destruction of Nascent FtsZ Rings. J. Bacteriol.
184: 2951-2962
[Abstract] [Full Text] -
Hu, Z., Gogol, E. P., Lutkenhaus, J.
(2002). Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE. Proc. Natl. Acad. Sci. USA
99: 6761-6766
[Abstract] [Full Text] -
Meinhardt, H., de Boer, P. A. J.
(2001). Pattern formation in Escherichia coli: A model for the pole-to-pole oscillations of Min proteins and the localization of the division site. Proc. Natl. Acad. Sci. USA
98: 14202-14207
[Abstract] [Full Text] -
Szeto, J., Ramirez-Arcos, S., Raymond, C., Hicks, L. D., Kay, C. M., Dillon, J.-A. R.
(2001). Gonococcal MinD Affects Cell Division in Neisseria gonorrhoeae and Escherichia coli and Exhibits a Novel Self-Interaction. J. Bacteriol.
183: 6253-6264
[Abstract] [Full Text] -
Charles, M., Perez, M., Kobil, J. H., Goldberg, M. B.
(2001). Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and Vibrio. Proc. Natl. Acad. Sci. USA
10.1073/pnas.171310498v1
[Abstract] [Full Text] -
Nanninga, N.
(2001). Cytokinesis in Prokaryotes and Eukaryotes: Common Principles and Different Solutions. Microbiol. Mol. Biol. Rev.
65: 319-333
[Abstract] [Full Text] -
RayChaudhuri, D., Gordon, G. S., Wright, A.
(2001). Protein acrobatics and bacterial cell polarity. Proc. Natl. Acad. Sci. USA
98: 1332-1334
[Full Text] -
Fu, X., Shih, Y.-L., Zhang, Y., Rothfield, L. I.
(2001). The MinE ring required for proper placement of the division site is a mobile structure that changes its cellular location during the Escherichia coli division cycle. Proc. Natl. Acad. Sci. USA
10.1073/pnas.031549298v1
[Abstract] [Full Text] -
Ramirez-Arcos, S., Szeto, J., Beveridge, T. J., Victor, C., Francis, F., Dillon, J.-A. R.
(2001). Deletion of the cell-division inhibitor MinC results in lysis of Neisseria gonorrhoeae. Microbiology
147: 225-237
[Abstract] [Full Text] -
Fu, X., Shih, Y.-L., Zhang, Y., Rothfield, L. I.
(2001). The MinE ring required for proper placement of the division site is a mobile structure that changes its cellular location during the Escherichia coli division cycle. Proc. Natl. Acad. Sci. USA
98: 980-985
[Abstract] [Full Text] -
Charles, M., Perez, M., Kobil, J. H., Goldberg, M. B.
(2001). Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and Vibrio. Proc. Natl. Acad. Sci. USA
98: 9871-9876
[Abstract] [Full Text]
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»