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spoOJ is required for normal chromosome segregation as well as the initiation of sporulation in Bacillus subtilis
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Lin DC-H, Levin PA, Grossman AD: Bipolar localization of a chromosome partition protein in Bacillus subtilis. Proc Natl Acad Sci USA 1997, 94:4721-4726. Demonstration that SpoOJ forms discrete foci with cells that are oriented towards the poles of the cell. Evidence suggests that SpoOJ's role in chromosome segregation is to bind to the chromosome in the vicinity of oriC to orient the origins away from the division plane.
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Lin, D.C.-H.1
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0030927986
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Direct evidence for active segregation of oriC regions of the Bacillus subtilis chromosome and colocalization with the SpoOJ partitioning protein
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Lewis PJ, Errington J: Direct evidence for active segregation of oriC regions of the Bacillus subtilis chromosome and colocalization with the SpoOJ partitioning protein. Mol Microbiol 1997, 25:945-954. This work demonstrates that, within the limits of resolution of fluorescence microscopy, oriC overlaps SpoOJ foci. This result suggests that the role of SpoOJ in segregation is to bind near or at oriC to deliver it to the pole of the cell.
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Mohl DA, Gober JW: Cell cycle-dependent polar localization of chromosome partitioning proteins in Caulobacter crescentus. Cell 1997, 88:675-604. This paper describes the isolation of parAB homologe from Caulobacter crescentus. Evidence is presented that these homologs are necessary for efficient chromosome segregation in this organism. The ParAB proteins are found predominantly at the cell poles and ParB binds to a sequence near the par genes.
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Mohl, D.A.1
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Gordon GS, Sitnikov D, Webb CD, Teleman A, Straight A, Losick R, Murray AW, Wright A: Chromosome and low copy plasmid segregation in E coli: visual evidence for distinct mechanisms. Cell 1997, 90:1113-1121. Application of the tandem lac operator-Lacl-GFP system to replicons of E. coli. This paper shows that an oriC is near each pole in newborn cells growing in rich media. In longer cells four oriCs are present, with a copy at each pole and two more near the cell center. In addition, these results show that, in cells that have one visible P1 or F, it is at the cell center, whereas cells that have two have one copy at the one quarter position and another at the three quarter position. Interestingly, P1 replicates randomly during the cell cycle whereas F replicates at a particular cell size. Treatment of cells with the division inhibitor cephalexin affects P1 segregation but not F or oriC. The results suggests that three independent segregation mechanisms exist. The results also suggest that positional information is present in at the quarter positions in newborn cells.
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Gordon, G.S.1
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Lutkenhaus J, Addinall SG: Bacterial cell division and the Z ring. Annu Rev Biochem 1997, 66:93-116. A comprehensive review of the role of FtsZ in cell division in E. coli and other bacteria. This review brings together genetic, biochemical and cytological evidences supporting the proposal that the Z ring functions as a cytoskeletal element that directs septatian in all prokaryotic organisms.
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Rothfield LI, Justice SS: Bacterial cell division: the cycle of the ring. Cell 1997, 88:581-584. A concise review of the process of septation focusing on the Z ring. This review highlights the major questions in the field.
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Rothfield, L.I.1
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Characterization of ftsZ from Mycoplasma pulmonis, an organism lacking a cell wall
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Wang X, Lutkenhaus J: Characterization of ftsZ from Mycoplasma pulmonis, an organism lacking a cell wall. J Bacteriol 1996, 178:2314-2319.
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Wang, X.1
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16
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0029864056
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Isolation of an ftsZ homolog from the Archaebacterium Halobacterium salinarium: Implications for the evolution of FtsZ and tubulin
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Margolin W, Wang R, Kumar M: Isolation of an ftsZ homolog from the Archaebacterium Halobacterium salinarium: implications for the evolution of FtsZ and tubulin. J Bacteriol 1996, 178:1320-1327.
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Wang X, Lutkenhaus J: FtsZ ring: the eubacterial division apparatus conserved in archaebacteria. Mol Microbiol 1996, 21:313-320. This paper characterizes ftsZ from Haloferax volcanii. Demonstrates that properties of the protein are conserved and that FtsZ is localized to the division site. Thus, although archaebacteria have some properties in common with eukaryotes, such as transcription factors, the division process is similar to that occurring in eubacteria.
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Mol Microbiol
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Wang, X.1
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Baumann P, Jackson SP: An archaebacterial homologue of the essential eubacterial cell division protein FtsZ. Proc Natl Acad Sci USA 1996, 93:6726-6730.
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Addinall SG, Bi E, Lutkenhaus J: FtsZ ring formation in fts mutants. J Bacteriol 1996, 178:3877-3884. The authors use indirect immunofluorescence microscopy to examine Z ring formation. Z rings are detected at midcell shortly after division and before constriction begins. Z rings are not detected in ftsZ temperature sensitive (Ts) mutants but are detected in ftsA (Ts), ftsl (Ts), and ftsQ (Ts) mutants, Z rings are not, however, detected at all possible positions. Nonetheless, these results indicate that FtsZ arrives at the division site early and suggest that the ftsA, ftsl and ftsQ genes function after ftsZ.
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J Bacteriol
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Addinall, S.G.1
Bi, E.2
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Ma X, Ehrhardt DW, Margolin W: Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein. Proc Natl Acad Sci USA 1996, 93:12998-13003. This paper reports the use of an FtsZ-GFP fusion for visualization of FtsZ in living cells. Although this fusion cannot replace ftsZ it can be used to tag structures that are formed. With low level expression, Z rings can be visualized, whereas at higher levels spirals and other structures can be observed. FtsA was also localized to the division site using the GFP fusion strategy.
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Proc Natl Acad Sci USA
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Ma, X.1
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Pogliano J, Pogliano K, Weiss DS, Losick R, Beckwith J: Inactivation of Ftsl inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites. Proc Natl Acad Sci USA 1997, 94:559-564. The authors use cephalexin, which inhibits Ftsl (PBP3), to examine the effect of blocking division on Z ring formation and compare this with the effect of an ftsl temperature sensitive (Ts) mutation. The ftsl mutation leads to filaments with Z rings located sporadically along the length of the filament. In contrast, cephalexin leads to filaments with only one or two Z rings. This latter clear result suggests that something is limiting Z ring formation in these filaments; however, the limiting factor is not known. It could be failure to form division sites, insufficient FtsZ or some type of control limiting Z ring formation.
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Pogliano, J.1
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Addinall SG, Lutkenhaus J: FtsZ spirals and arcs determine the shape of the invaginating septa in some mutants of Escherichia coll. Mol Microbiol 1996, 22:231-238. This paper presents evidence that FtsZ structures determine septal morphology. The ftsZ26 mutation results in Z spirals that result in spiral septa. Also, in spherical mutants partial Z rings can be observed. Interestingly, the results demonstrate that septation begins before the ring is complete.
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Mol Microbiol
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Addinall, S.G.1
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Mukherjee A, Lutkenhaus J: Guanine nucleotide-dependent assembly of FtsZ into filaments. J Bacteriol 1994, 176:2754-2758.
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0030068218
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Bacterial cell division protein FtsZ assembles into protofilament sheet and minirings, structural homologs of tubulin polymers
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Erickson HP, Taylor DW, Taylor KA, Bramhill D: Bacterial cell division protein FtsZ assembles into protofilament sheet and minirings, structural homologs of tubulin polymers. Proc Natl Acad Sci USA 1996, 93:519-523. The authors use DEAE dextran or cationic lipids to promote FtsZ assembly into protofilaments, sheets and minirings. Optical diffraction of the sheets allows the structure of the protofilaments to be determined and compared to that of microtubules.
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Erickson, H.P.1
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Addinall SG, Lutkenhaus J: FtsA is localized to the septum in an FtsZ dependent manner. J Bacteriol 1996, 178:7167-7172. FtsA is localized to the septum coincident with FtsZ but its localization is clearly dependent upon prior FtsZ localization. Along with [18] this paper begins to establish an order to the addition of proteins to the division site.
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Ma X, Sun Q, Wang R, Singh G, Jonietz El, Margolin W: Interactions between heterologous FtsA and FtsZ proteins at the FtsZ ring. J Bacteriol 1997, 179:6788-6797. Further demonstration of the uses of GFP fusion technology to the study of protein localization. This paper shows that heterologous FtsZs can localize to the endogenous Z ring; however, heterologous FtsAs only localize if their cognate FtsZ is present.
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FtsN, a late recruit to the septum in E. coli
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Mol Microbiol
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Addinall, S.G.1
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Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole
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Weiss DS, Pogliano K, Carson M, Guzman LM, Fraipont C, Nguyen Disteche M, Losick R, Beckwitn J: Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole. Mol Microbiol 1997, 25:671-681. Using immunofluorescence microscopy it is demonstrated that Ftsl is localized to the division site, Ftsl is the least abundant protein that has been localized in bacteria using indirect immunofluorescence microscopy-∼50 molecules per cell.
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Raskin, D.M.1
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Levin, P.A.1
Losick, R.2
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Deletion of the Bacillus subtilis isocitrate dehydrogenase gene causes a block at stage I of sporulation
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Jin S, Levin PA, Matsuno K, Grossman AD, Sonenshein AL: Deletion of the Bacillus subtilis isocitrate dehydrogenase gene causes a block at stage I of sporulation. J Bacteriol 1997, 179:4725-4732. This paper shows that deletion of the gene for isocitrate dehydrogenase blocks the sporulation pathway after formation of the polar Z rings, a similar phenotype to that of spoOH mutants. This indicates that Z rings are stable under some conditions and that the initiation of constriction of the Z ring is regulated.
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Temperature shift experiments with an ftsZ84 (Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated
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Addnall SG, Cao C, Lutkenhaus J: Temperature shift experiments with an ftsZ84 (Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated. J Bacteriol 1997, 179:4277-4284. This paper reports several interesting observations about FtsZ localization following temperature shifts with an ftsZ84 temperature sensitive (Ts) strain. Shifting to nonpermissive temperature blocks FtsZ localization; however, FtsZ rapidly localizes after a shift to permissive temperature. The regular spacing of FtsZ suggests that nucleation sites were formed at nonpermissive temperature. FtsZ did not, however, return to sites that had begun constriction before the temperature shift.
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J Bacteriol
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Addnall, S.G.1
Cao, C.2
Lutkenhaus, J.3
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ftsW is an essential cell division gene in Escherichia coli
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Boyle DS, Khattar MM, Addinall SG, Lutkenhaus J, Donachie WD: ftsW is an essential cell division gene in Escherichia coli. Mol Microbiol 1997, 24:1263-1273.
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Lutkenhaus, J.4
Donachie, W.D.5
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Cell division inhibitors SulA and MinCD prevent formation of the FtsZ ring
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Bi E, Lutkenhaus J: Cell division inhibitors SulA and MinCD prevent formation of the FtsZ ring. J Bacteriol 1993, 175:1118-1125.
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Lutkenhaus, J.2
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Interaction between FtsZ and inhibitors of cell division
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Huang J, Cao C, Lutkenhaus J: Interaction between FtsZ and inhibitors of cell division. J Bacteriol 1996, 178:5080-5085. The authors use of the yeast two-hybrid system to examine interaction among cell division inhibitors and FtsZ, FtsZ interacts with SulA but not with MinCD. Most of the mutations in ftsZ and sulA that prevent inhibition of division prevent interaction in this test system. Furthermore, MinC and MinE both interact with MinD as suggested by earlier genetic studies.
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A cell division inhibitor SulA of Escherichia coli directly interacts with FtsZ through GTP hydrolysis
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Higashitani A, Higashitani N, Horiughi K: A cell division inhibitor SulA of Escherichia coli directly interacts with FtsZ through GTP hydrolysis. Biochem Biophys Res Commun 1995, 209:198-204.
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sfi-independent filamentation in Escherichia coli is lexA dependent and requires DNA damage for induction
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Hill TM, Sharma B, Valjavec-Gratian M, Smith J: sfi-independent filamentation in Escherichia coli is lexA dependent and requires DNA damage for induction. J Bacteriol 1997, 179:1931-1939. These authors examine division inhibition following DNA damage and find evidence for a new inhibitor that, like sulA, is part of the SOS response. Although SulA is active as soon as it is expressed the second inhibitor must be expressed and subsequently activated by the DNA damage.
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J Bacteriol
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Hill, T.M.1
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