title: Localization of FtsZ in Helicobacter pylori and consequences for cell division.
abstract: Of the various kinds of cell division, the most common mode is binary fission, the division of a cell into two morphologically identical daughter cells. However, in the case of asymmetric cell division, Caulobacter crescentus produces two morphologically and functionally distinct cell types. Here, we have studied cell cycle progression of the human pathogen Helicobacter pylori using a functional green fluorescent protein (GFP) fusion of FtsZ protein and membrane staining. In small cells, representing newly divided cells, FtsZ localizes to a single cell pole. During the cell cycle, spiral intermediates are formed until an FtsZ ring is positioned with very little precision, such that central as well as acentral rings can be observed. Daughter cells showed considerably different sizes, suggesting that H. pylori divides asymmetrically. Fluorescence recovery after photobleaching (FRAP) analyses demonstrate that the H. pylori FtsZ ring is about as dynamic as that of Escherichia coli but that polar assemblies show less turnover. Strikingly, our results demonstrate that H. pylori cell division follows a different route from that in E. coli and Bacillus subtilis. It is also different from that in C. crescentus, where cytokinesis regulation proteins like MipZ play a role. Therefore, this report provides the first cell-biological analysis of FtsZ dynamics in the human pathogen H. pylori and even in epsilonproteobacteria to our knowledge. In addition, analysis of the filament architecture of H. pylori and E. coli FtsZ filaments in the heterologous system of Drosophila melanogaster S2 Schneider cells revealed that both have different filamentation properties in vivo, suggesting a unique intrinsic characteristic of each protein.
authors: Department of Medical Microbiology and Hygiene, Institute of Medical Microbiology and Hygiene, University Hospital Freiburg, Freiburg, Germany.
authors: Mara
authors: M
authors: Specht
authors: Felix
authors: F
authors: Dempwolff
authors: Sarah
authors: S
authors: Schätzle
authors: Ralf
authors: R
authors: Thomann
authors: Barbara
authors: B
authors: Waidner
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis* / Q000235:genetics; D002455:Cell Division; D003598:Cytoskeletal Proteins / Q000032:analysis* / Q000235:genetics; D017930:Genes, Reporter; D049452:Green Fluorescent Proteins / Q000032:analysis / Q000235:genetics; D016480:Helicobacter pylori / Q000737:chemistry* / Q000166:cytology / Q000378:metabolism / Q000502:physiology*; D011993:Recombinant Fusion Proteins / Q000032:analysis / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins