Membrane Redistribution of the Escherichia coli MinD Protein Induced by MinE
AUTOR(ES)
Rowland, S. L.
FONTE
American Society for Microbiology
RESUMO
Escherichia coli cells contain potential division sites at midcell and adjacent to the cell poles. Selection of the correct division site at midcell is controlled by three proteins: MinC, MinD, and MinE. It has previously been shown (D. Raskin and P. de Boer, Cell 91:685–694, 1997) that MinE-Gfp localizes to the midcell site in an MinD-dependent manner. We use here Gfp-MinD to show that MinD associates with the membrane around the entire periphery of the cell in the absence of the other Min proteins and that MinE is capable of altering the membrane distribution pattern of Gfp-MinD. Studies with the isolated N-terminal and C-terminal MinE domains indicated different roles for the two MinE domains in the redistribution of membrane-associated MinD.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=94322Documentos Relacionados
- Mapping the MinE Site Involved in Interaction with the MinD Division Site Selection Protein of Escherichia coli
- Recruitment of MinC, an Inhibitor of Z-Ring Formation, to the Membrane in Escherichia coli: Role of MinD and MinE
- Dynamic structures in Escherichia coli: Spontaneous formation of MinE rings and MinD polar zones
- Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE
- Analysis of MinD Mutations Reveals Residues Required for MinE Stimulation of the MinD ATPase and Residues Required for MinC Interaction