title: Dynamics of FtsZ assembly during sporulation in Streptomyces coelicolor A3(2).
abstract: FtsZ, the bacterial tubulin homologue, is the main player in at least two distinct processes of cell division during the development of Streptomyces coelicolor A3(2). It forms cytokinetic rings and is required for the formation of both the widely spaced hyphal cross walls in the substrate mycelium and the specialized septation that converts sporogenic aerial hyphae into spores. The latter developmentally controlled septation involves the coordinated assembly of large numbers of FtsZ rings in each sporulating hyphal cell. We used an FtsZ-enhanced green fluorescent protein (EGFP) translational fusion to visualize the progression of FtsZ ring assembly in vivo during sporulation of aerial hyphae. This revealed that the regular placement of multiple FtsZ rings and initiation of cytokinesis was preceded by a protracted phase during which spiral-shaped FtsZ intermediates were detected along the length of the aerial hyphal cell. Time course experiments indicated that they were remodeled and gradually replaced by regularly spaced FtsZ rings. Such spiral-shaped filaments could also be detected with immunofluorescence microscopy using an antiserum against FtsZ. Based on our observations, we propose a model for the progression of Z-ring assembly during sporulation of S. coelicolor. Furthermore, mutants lacking the developmental regulatory genes whiA, whiB, whiG, whiH, and whiI were investigated. They failed in up-regulation of the expression of FtsZ-EGFP in aerial hyphae, which is consistent with the known effects of these genes on ftsZ transcription.
authors.affiliation: Dept. of Cell and Organism Biology, Uppsala University, SE-751 24 Uppsala, Sweden.
authors.forename: Nina
authors.initials: N
authors.lastname: Grantcharova
authors.forename: Ulrika
authors.initials: U
authors.lastname: Lustig
authors.forename: Klas
authors.initials: K
authors.lastname: Flärdh
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D001704:Biopolymers / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000032:analysis* / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000235:genetics / Q000502:physiology; D049452:Green Fluorescent Proteins / Q000235:genetics; D008856:Microscopy, Fluorescence; D009154:Mutation; D011993:Recombinant Fusion Proteins / Q000235:genetics; D012097:Repressor Proteins / Q000235:genetics / Q000502:physiology; D012808:Sigma Factor / Q000235:genetics / Q000502:physiology; D013171:Spores, Bacterial / Q000235:genetics / Q000254:growth & development*; D048372:Streptomyces coelicolor / Q000235:genetics / Q000502:physiology*; D014157:Transcription Factors / Q000235:genetics / Q000502:physiology
chemical_list: D001426:Bacterial Proteins; D001704:Biopolymers; D003598:Cytoskeletal Proteins; D004268:DNA-Binding Proteins; C071525:FtsZ protein, Bacteria; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins; D012808:Sigma Factor; D014157:Transcription Factors; C414486:WhiA protein, Streptomyces coelicolor; C081543:whiB protein, Streptomyces; C115233:whiH protein, Streptomyces; C061314:whiG protein, Streptomyces coelicolor; D049452:Green Fluorescent Proteins