title: Mapping the MinE site involved in interaction with the MinD division site selection protein of Escherichia coli.
abstract: Interactions between the MinD and MinE proteins are required for proper placement of the Escherichia coli division septum. The site within MinE that is required for interaction with MinD was mapped by studying the effects of site-directed minE mutations on MinD-MinE interactions in yeast two-hybrid and three-hybrid experiments. This confirmed that the MinE N-terminal domain is responsible for the interaction of MinE with MinD. Mutations that interfered with the interaction defined an extended surface on one face of the alpha-helical region of the MinE N-terminal domain, consistent with the idea that the MinE-MinD interaction involves formation of a coiled-coil structure by interaction with a complementary helical surface within MinD.
authors.affiliation: Department of Microbiology, University of Connecticut Health Center, Farmington, Connecticut 06032, USA.
authors.forename: Lu-Yan
authors.initials: LY
authors.lastname: Ma
authors.forename: Glenn
authors.initials: G
authors.lastname: King
authors.forename: Lawrence
authors.initials: L
authors.lastname: Rothfield
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D018797:Cell Cycle Proteins; D002455:Cell Division; D002462:Cell Membrane / Q000378:metabolism; D004926:Escherichia coli / Q000166:cytology* / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D008856:Microscopy, Fluorescence; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D020798:Two-Hybrid System Techniques
chemical_list: D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; C093548:MinE protein, E coli; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli