title: The Min oscillator uses MinD-dependent conformational changes in MinE to spatially regulate cytokinesis.
abstract: In E. coli, MinD recruits MinE to the membrane, leading to a coupled oscillation required for spatial regulation of the cytokinetic Z ring. How these proteins interact, however, is not clear because the MinD-binding regions of MinE are sequestered within a six-stranded β sheet and masked by N-terminal helices. minE mutations that restore interaction between some MinD and MinE mutants were isolated. These mutations alter the MinE structure leading to release of the MinD-binding regions and the N-terminal helices that bind the membrane. Crystallization of MinD-MinE complexes revealed a four-stranded β sheet MinE dimer with the released β strands (MinD-binding regions) converted to α helices bound to MinD dimers. These results identify the MinD-dependent conformational changes in MinE that convert it from a latent to an active form and lead to a model of how MinE persists at the MinD-membrane surface.
authors.affiliation: Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, KS 66160, USA.
authors.forename: Kyung-Tae
authors.initials: KT
authors.lastname: Park
authors.forename: Wei
authors.initials: W
authors.lastname: Wu
authors.forename: Kevin P
authors.initials: KP
authors.lastname: Battaile
authors.forename: Scott
authors.initials: S
authors.lastname: Lovell
authors.forename: Todd
authors.initials: T
authors.lastname: Holyoak
authors.forename: Joe
authors.initials: J
authors.lastname: Lutkenhaus
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D001483:Base Sequence; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018360:Crystallography, X-Ray; D048749:Cytokinesis; D004926:Escherichia coli / Q000166:cytology* / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006090:Gram-Negative Bacteria / Q000378:metabolism; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017433:Protein Structure, Secondary; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; C093548:MinE protein, E coli; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli