Literature DB >> 11029443

Deletion of the min operon results in increased thermosensitivity of an ftsZ84 mutant and abnormal FtsZ ring assembly, placement, and disassembly.

X C Yu1, W Margolin.   

Abstract

To investigate the interaction between FtsZ and the Min system during cell division of Escherichia coli, we examined the effects of combining a well-known thermosensitive mutation of ftsZ, ftsZ84, with DeltaminCDE, a deletion of the entire min locus. Because the Min system is thought to down-regulate Z-ring assembly, the prediction was that removing minCDE might at least partially suppress the thermosensitivity of ftsZ84, which can form colonies below 42 degrees C but not at or above 42 degrees C. Contrary to expectations, the double mutant was significantly more thermosensitive than the ftsZ84 single mutant. When shifted to the new lower nonpermissive temperature, the double mutant formed long filaments mostly devoid of Z rings, suggesting a likely cause of the increased thermosensitivity. Interestingly, even at 22 degrees C, many Z rings were missing in the double mutant, and the rings that were present were predominantly at the cell poles. Of these, a large number were present only at one pole. These cells exhibited a higher than expected incidence of polar divisions, with a bias toward the newest pole. Moreover, some cells exhibited dramatically elongated septa that stained for FtsZ, suggesting that the double mutant is defective in Z-ring disassembly, and providing a possible mechanism for the polar bias. Thermoresistant suppressors of the double mutant arose that had modestly increased levels of FtsZ84. These cells also exhibited elongated septa and, in addition, produced a high frequency of branched cells. A thermoresistant suppressor of the ftsZ84 single mutant also synthesized more FtsZ84 and produced branched cells. The evidence from this study indicates that removing the Min system exposes and exacerbates the inherent defects of the FtsZ84 protein, resulting in clear septation phenotypes even at low growth temperatures. Increasing levels of FtsZ84 can suppress some, but not all, of these phenotypes.

Entities:  

Mesh:

Substances:

Year:  2000        PMID: 11029443      PMCID: PMC94757          DOI: 10.1128/JB.182.21.6203-6213.2000

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  42 in total

1.  FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli.

Authors:  L M Guzman; J J Barondess; J Beckwith
Journal:  J Bacteriol       Date:  1992-12       Impact factor: 3.490

2.  The essential bacterial cell-division protein FtsZ is a GTPase.

Authors:  P de Boer; R Crossley; L Rothfield
Journal:  Nature       Date:  1992-09-17       Impact factor: 49.962

3.  Isolation and characterization of ftsZ alleles that affect septal morphology.

Authors:  E Bi; J Lutkenhaus
Journal:  J Bacteriol       Date:  1992-08       Impact factor: 3.490

4.  Interaction between FtsZ and inhibitors of cell division.

Authors:  J Huang; C Cao; J Lutkenhaus
Journal:  J Bacteriol       Date:  1996-09       Impact factor: 3.490

5.  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.

Authors:  S G Addinall; C Cao; J Lutkenhaus
Journal:  J Bacteriol       Date:  1997-07       Impact factor: 3.490

6.  Conserved cell and organelle division.

Authors:  K W Osteryoung; E Vierling
Journal:  Nature       Date:  1995-08-10       Impact factor: 49.962

7.  Analysis of ftsZ mutations that confer resistance to the cell division inhibitor SulA (SfiA).

Authors:  E Bi; J Lutkenhaus
Journal:  J Bacteriol       Date:  1990-10       Impact factor: 3.490

8.  Cell division in Escherichia coli minB mutants.

Authors:  T Akerlund; R Bernander; K Nordström
Journal:  Mol Microbiol       Date:  1992-08       Impact factor: 3.501

9.  Cell division inhibitors SulA and MinCD prevent formation of the FtsZ ring.

Authors:  E Bi; J Lutkenhaus
Journal:  J Bacteriol       Date:  1993-02       Impact factor: 3.490

10.  Branched Escherichia coli cells.

Authors:  T Akerlund; K Nordström; R Bernander
Journal:  Mol Microbiol       Date:  1993-11       Impact factor: 3.501

View more
  26 in total

1.  Exploring intracellular space: function of the Min system in round-shaped Escherichia coli.

Authors:  Brian D Corbin; Xuan-Chuan Yu; William Margolin
Journal:  EMBO J       Date:  2002-04-15       Impact factor: 11.598

2.  FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli.

Authors:  Swapna Thanedar; William Margolin
Journal:  Curr Biol       Date:  2004-07-13       Impact factor: 10.834

3.  FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli.

Authors:  Archana Varma; Kevin D Young
Journal:  J Bacteriol       Date:  2004-10       Impact factor: 3.490

4.  Evidence for functional overlap among multiple bacterial cell division proteins: compensating for the loss of FtsK.

Authors:  Brett Geissler; William Margolin
Journal:  Mol Microbiol       Date:  2005-10       Impact factor: 3.501

Review 5.  The selective value of bacterial shape.

Authors:  Kevin D Young
Journal:  Microbiol Mol Biol Rev       Date:  2006-09       Impact factor: 11.056

6.  Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring.

Authors:  Daisuke Shiomi; William Margolin
Journal:  Mol Microbiol       Date:  2007-11-06       Impact factor: 3.501

7.  Peptide Linkers within the Essential FtsZ Membrane Tethers ZipA and FtsA Are Nonessential for Cell Division.

Authors:  Kara M Schoenemann; Daniel E Vega; William Margolin
Journal:  J Bacteriol       Date:  2020-02-25       Impact factor: 3.490

8.  A mutation in Escherichia coli ftsZ bypasses the requirement for the essential division gene zipA and confers resistance to FtsZ assembly inhibitors by stabilizing protofilament bundling.

Authors:  Daniel P Haeusser; Veronica W Rowlett; William Margolin
Journal:  Mol Microbiol       Date:  2015-07-04       Impact factor: 3.501

9.  The MinCDJ system in Bacillus subtilis prevents minicell formation by promoting divisome disassembly.

Authors:  Suey van Baarle; Marc Bramkamp
Journal:  PLoS One       Date:  2010-03-24       Impact factor: 3.240

10.  ClpXP and ClpAP control the Escherichia coli division protein ZapC by proteolysis.

Authors:  Monika S Buczek; Andrea L Cardenas Arevalo; Anuradha Janakiraman
Journal:  Microbiology       Date:  2016-03-15       Impact factor: 2.777

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.