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Recruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE.

publicado en: Journal of Bacteriology

fecha de publicación: 2003-01-01

idioma: inglés

tema principal: Escherichia coli

Cites articles 36

Fecha

Título

Autores

2003-01-01

A conserved sequence at the C-terminus of MinD is required for binding to the membrane and targeting MinC to the septum
2002-05-14

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE
2002-07-01

Division site placement in E.coli: mutations that prevent formation of the MinE ring lead to loss of the normal midcell arrest of growth of polar MinD membrane domains

Glenn F King
2002-06-01

Targeting of (D)MinC/MinD and (D)MinC/DicB complexes to septal rings in Escherichia coli suggests a multistep mechanism for MinC-mediated destruction of nascent FtsZ rings

Piet de Boer
2001-05-01

Crystal structure of the bacterial cell division inhibitor MinC.
2001-04-01

Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus

Takuji Oyama
2001-03-09

Crystal structure of the bacterial cell division regulator MinD
2001-12-01

Pattern formation in Escherichia coli: a model for the pole-to-pole oscillations of Min proteins and the localization of the division site
2001-11-01

The dimerization function of MinC resides in a structurally autonomous C-terminal domain

Susan L Rowland, Glenn F King
2001-11-01

Escherichia coli division inhibitor MinCD blocks septation by preventing Z-ring formation
2001-11-01

Gonococcal MinD affects cell division in Neisseria gonorrhoeae and Escherichia coli and exhibits a novel self-interaction
2001-06-01

Topological regulation of cell division in E. coli. spatiotemporal oscillation of MinD requires stimulation of its ATPase by MinE and phospholipid
2001-04-01

Dynamic localization cycle of the cell division regulator MinE in Escherichia coli
2001-01-23

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
2000-10-01

Themes and variations in prokaryotic cell division
2000-07-01

Analysis of MinC reveals two independent domains involved in interaction with MinD and FtsZ
2000-07-01

Cell division inhibitors SulA and MinC/MinD block septum formation at different steps in the assembly of the Escherichia coli division machinery

Jorge García-Lara
1999-04-27

Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli
1999-12-01

The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization
1999-10-01

MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli

David Raskin, Piet de Boer
1999-02-01

The dimerization and topological specificity functions of MinE reside in a structurally autonomous C-terminal domain

Glenn F King, Susan L Rowland, Joel P Mackay
1999-04-01

FtsZ ring clusters in min and partition mutants: role of both the Min system and the nucleoid in regulating FtsZ ring localization
1999-10-01

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
1997-05-22

Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction

Hermann Schindelin
1997-11-01

The MinE ring: an FtsZ-independent cell structure required for selection of the correct division site in E. coli

David Raskin, Piet de Boer
1997-01-01

Bacterial cell division and the Z ring
1996-09-01

Interaction between FtsZ and inhibitors of cell division
1995-10-01

Deletion analysis of gene minE which encodes the topological specificity factor of cell division in Escherichia coli
1995-05-01

Proper placement of the Escherichia coli division site requires two functions that are associated with different domains of the MinE protein

Piet de Boer
1993-02-01

A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif

Eugene Koonin
1993-02-01

Cell division inhibitors SulA and MinCD prevent formation of the FtsZ ring
1992-01-01

Roles of MinC and MinD in the site-specific septation block mediated by the MinCDE system of Escherichia coli

Piet de Boer

Artículo - wd:Q24541591

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