Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli.

doi:10.1111/j.1365-2958.2009.07006.x

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Article

Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli.

Molecular microbiology - 1 Jan 2010

Hsieh Cheng-Wei, Lin Ti-Yu, Lai Hsin-Mei, Lin Chu-Chi, Hsieh Ting-Sung, Shih Yu-Ling

Abstract excerpt

Dynamic oscillation of the Min system in Escherichia coli determines the placement of the division plane at the midcell. In addition to stimulating MinD ATPase activity, we report here that MinE can directly interact with the membrane and this interaction contributes to the proper MinDE localization and dynamics. The N-terminal domain of MinE is involved in direct contact between MinE and the membranes that may...

Topics

Adenosine Triphosphatases
Amino Acid Sequence
Cell Cycle Proteins
Cell Division
Cell Membrane
Escherichia coli
Escherichia coli Proteins
Kinetics
Liposomes
Molecular Sequence Data
Mutagenesis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protein Binding

Sequence Alignment

Sequence Homology, Amino Acid

Solutions

Static Electricity

Source

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Identifiers

PMID: 20025670
DOI: 10.1111/j.1365-2958.2009.07006.x
PMCID: PMC2814086

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Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli.PMID 20025670Read ↗

MinE conformational dynamics regulate membrane binding, MinD interaction, and Min oscillation.Semantic proximity Read ↗

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.Semantic proximity Read ↗

A conserved polar region in the cell division site determinant MinD is required for responding to MinE-induced oscillation but not for localization within coiled arrays.Semantic proximity Read ↗

Membrane redistribution of the Escherichia coli MinD protein induced by MinE.Semantic proximity Read ↗

Large-scale modulation of reconstituted Min protein patterns and gradients by defined mutations in MinE's membrane targeting sequence.Semantic proximity Read ↗

Proper placement of the Escherichia coli division site requires two functions that are associated with different domains of the MinE protein.Semantic proximity Read ↗

A multistranded polymer model explains MinDE dynamics in E. coli cell division.Semantic proximity Read ↗

A plant MinD homologue rescues Escherichia coli HL1 mutant (DeltaMinDE) in the absence of MinE.Semantic proximity Read ↗

Roles of MinC and MinD in the site-specific septation block mediated by the MinCDE system of Escherichia coli.Semantic proximity Read ↗

The switch I and II regions of MinD are required for binding and activating MinC.Semantic proximity Read ↗

Mapping the MinE site involved in interaction with the MinD division site selection protein of Escherichia coli.Semantic proximity Read ↗

The N terminus of MinD contains determinants which affect its dynamic localization and enzymatic activity.Semantic proximity Read ↗

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