title: The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation.
abstract: Establishment of an axis of cell polarity and differentiation of the cell poles are fundamental aspects of cellular development in many organisms. We compared the effects of two bacterial cytoskeletal-like systems, the MreB and MinCDE systems, on these processes in Escherichia coli. We report that the Min proteins are capable of establishing an axis of oscillation that is the initial step in establishment of polarity in spherical cells, in a process that is independent of the MreB cytoskeleton. In contrast, the MreB system is required for establishment of the rod shape of the cell and for polar targeting of other polar constituents, such as the Shigella virulence factor IcsA and the aspartate chemoreceptor Tar, in a process that is independent of the Min system. Thus, the two bacterial cytoskeletal-like systems act independently on different aspects of cell polarization.
authors.affiliation: Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, Farmington, CT 06032, USA. ylshih@neuron.uchc.edu
authors.forename: Yu-Ling
authors.initials: YL
authors.lastname: Shih
authors.forename: Ikuro
authors.initials: I
authors.lastname: Kawagishi
authors.forename: Lawrence
authors.initials: L
authors.lastname: Rothfield
mesh_terms: D000251:Adenosine Triphosphatases / Q000032:analysis / Q000235:genetics / Q000502:physiology; D001426:Bacterial Proteins / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000032:analysis / Q000235:genetics / Q000502:physiology; D002628:Chemoreceptor Cells; D004268:DNA-Binding Proteins / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry / Q000166:cytology* / Q000235:genetics / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000032:analysis / Q000235:genetics* / Q000378:metabolism / Q000502:physiology*; D017353:Gene Deletion; D049452:Green Fluorescent Proteins / Q000032:analysis / Q000235:genetics; D008565:Membrane Proteins / Q000032:analysis / Q000235:genetics / Q000502:physiology; D008856:Microscopy, Fluorescence; D008954:Models, Biological; D016254:Mutagenesis, Insertional; D011956:Receptors, Cell Surface / Q000378:metabolism; D012760:Shigella / Q000166:cytology / Q000235:genetics / Q000502:physiology; D013194:Staining and Labeling; D014157:Transcription Factors / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C462942:MinC protein, E coli; C093548:MinE protein, E coli; D011956:Receptors, Cell Surface; C057331:Tar protein, E coli; D014157:Transcription Factors; C058483:virG protein, Shigella flexneri; D049452:Green Fluorescent Proteins; C078473:MreB protein, E coli; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli