MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ.

No abstract is available for this paper.

• Publication year

  2008

• Venue

  Current Biology

• Publication date

  2008-02-26

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/j.cub.2008.01.042PMID 18291654
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring.

  2007cited by this paper
• FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP.

  2007cited by this paper
• FtsZ from Divergent Foreign Bacteria Can Function for Cell Division in Escherichia coli

  2006influential reference
• Structural mechanisms underlying nucleotide-dependent self-assembly of tubulin and its relatives.

  2006cited by this paper
• MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter.

  2006influential reference
• Z Ring as Executor of Bacterial Cell Division

  2006influential reference
• The C-Terminal Domain of MinC Inhibits Assembly of the Z Ring in Escherichia coli

  2006cited by this paper
• The rapid onset of elasticity during the assembly of the bacterial cell-division protein FtsZ.

  2005cited by this paper
• Rapid in Vitro Assembly Dynamics and Subunit Turnover of FtsZ Demonstrated by Fluorescence Resonance Energy Transfer*

  2005cited by this paper
• MinC Mutants Deficient in MinD- and DicB-Mediated Cell Division Inhibition Due to Loss of Interaction with MinD, DicB, or a Septal Component

  2005cited by this paper
• The Switch I and II Regions of MinD Are Required for Binding and Activating MinC

  2004cited by this paper
• ZipA Is Required for Targeting of DMinC/DicB, but Not DMinC/MinD, Complexes to Septal Ring Assemblies in Escherichia coli

  2004cited by this paper
• The crystal structure of ZapA and its modulation of FtsZ polymerisation.

  2004cited by this paper
• EzrA prevents aberrant cell division by modulating assembly of the cytoskeletal protein FtsZ

  2004cited by this paper
• Assembly Dynamics of FtsZ Rings in Bacillus subtilis and Escherichia coli and Effects of FtsZ-Regulating Proteins

  2004cited by this paper
• FtsZ Fiber Bundling Is Triggered by a Conformational Change in Bound GTP*

  2004cited by this paper
• Recruitment of MinC, an Inhibitor of Z-Ring Formation, to the Membrane in Escherichia coli: Role of MinD and MinE

  2003cited by this paper
• ATP-Dependent Interactions between Escherichia coli Min Proteins and the Phospholipid Membrane In Vitro

  2003cited by this paper
• Membrane Binding by MinD Involves Insertion of Hydrophobic Residues within the C-Terminal Amphipathic Helix into the Bilayer

  2003cited by this paper
• Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

  2002cited by this paper
• Immediate GTP hydrolysis upon FtsZ polymerization

  2002cited by this paper
• A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ.

  2002influential reference
• 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

  2002cited by this paper
• GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers.

  2002cited by this paper
• Crystal structure of the bacterial cell division inhibitor MinC

  2001cited by this paper
• Dynamic localization cycle of the cell division regulator MinE in Escherichia coli

  2001cited by this paper
• Cell division inhibitors SulA and MinC/MinD block septum formation at different steps in the assembly of the Escherichia coli division machinery

  2000cited by this paper
• Analysis of MinC Reveals Two Independent Domains Involved in Interaction with MinD and FtsZ

  2000cited by this paper
• MinDE-Dependent Pole-to-Pole Oscillation of Division Inhibitor MinC in Escherichia coli

  1999cited by this paper
• Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli.

  1999cited by this paper
• Topological regulation of cell division in Escherichia coli involves rapid pole to pole oscillation of the division inhibitor MinC under the control of MinD and MinE

  1999cited by this paper
• The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization.

  1999cited by this paper
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• Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site.

  1998cited by this paper
• 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

  1997cited by this paper
• Physical Chemistry of Macromolecules

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• The ATP-dependent protease ClpYQ degrades cell division proteins DivIVA and Mbl in Bacillus subtilis

  2024cites this paper
• NMR study of the interaction between MinC and FtsZ and modeling of the FtsZ:MinC complex

  2024influential citation
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• Bacterial division ring stabilizing ZapA versus destabilizing SlmA modulate FtsZ switching between biomolecular condensates and polymers

  2023cites this paper
• The C‐terminal domain of MinC, a cell division regulation protein, is sufficient to form a copolymer with MinD

  2023influential citation
• Models versus pathogens: how conserved is the FtsZ in bacteria?

  2023cites this paper
• Benzodioxane-benzamides as promising inhibitors of Escherichia coli FtsZ.

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• Residue 49 of AtMinD1 Plays a Key Role in the Guidance of Chloroplast Division by Regulating the ARC6-AtMinD1 Interaction

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• The Stress-Active Cell Division Protein ZapE Alters FtsZ Filament Architecture to Facilitate Division in Escherichia coli

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• FtsZ Interactions and Biomolecular Condensates as Potential Targets for New Antibiotics

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• Cell division protein FtsZ: from structure and mechanism to antibiotic target.

  2020cites this paper
• Quantification of Predictive Uncertainty in Models of FtsZ ring assembly in Escherichia coli.

  2020cites this paper
• Dynamics of the Bacillus subtilis Min System

  2020cites this paper
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  2020cites this paper
• Bulk-surface coupling reconciles Min-protein pattern formation in vitro and in vivo

  2020cites this paper
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  2020cites this paper
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  2019cites this paper
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  2019cites this paper
• THE SPATIAL ORGANIZATION OF MYCOBACTERIAL MEMBRANE

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  2019cites this paper
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  2019cites this paper
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  2018cites this paper
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  2018cites this paper
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  2018cites this paper
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  2018cites this paper
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  2018cites this paper
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  2018cites this paper
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  2018cites this paper
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  2018cites this paper
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  2018cites this paper
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  2018cites this paper
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  2018cites this paper
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  2018cites this paper
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  2018influential citation
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  2018cites this paper
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  2018cites this paper
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  2018cites this paper
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  2018cites this paper
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  2017cites this paper
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  2017cites this paper
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  2017cites this paper
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  2017cites this paper
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  2017cites this paper
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  2017cites this paper
• Bacterial inner membrane remodelling by force generation of FtsZ fibres

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  2016cites this paper
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  2016cites this paper
• An intrinsically disordered linker plays a critical role in bacterial cell division.

  2015cites this paper
• ZapC promotes assembly and stability of FtsZ filaments by binding at a different site on FtsZ than ZipA.

  2015cites this paper
• The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide

  2015cites this paper
• MinC/MinD copolymers are not required for Min function

  2015influential citation
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  2015cites this paper
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  2015cites this paper
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  2014cites this paper
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  2014influential citation
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  2014cites this paper
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  2014cites this paper
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  2014cites this paper