title: A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis.
abstract: The assembly of ring-like structures, composed of FtsZ proteins (i.e. the Z ring), is the earliest and most essential process in bacterial cytokinesis. It has been shown that this process is directly regulated by the FtsZ-binding proteins, FtsA, ZapA, and EzrA, in Bacillus subtilis. In this study, protein complexes that are involved in Z-ring formation were chemically cross-linked in vivo, purified by affinity chromatography, and analysed by mass spectrometry. Analysis of the results identified YlmF as a new component of the FtsZ complex. Yeast two-hybrid analysis and fluorescence microscopy of YFP-YlmF in B. subtilis cells indicated YlmF localizes to the division site in an FtsZ-dependent manner. A single disruption of YlmF resulted in a slight elongation of cells; however, simultaneous inactivation of both YlmF and FtsA showed synthetic lethality caused by complete blockage of cell division due to the defect in Z-ring formation. In contrast, the ftsA-null mutant phenotype, caused by inefficient Z-ring formation, could be complemented by overexpression of YlmF. These results suggest that YlmF has an overlapping function with FtsA in stimulating the formation of Z rings in B. subtilis.
authors.affiliation: Graduate School of Information Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0101, Japan.
authors.forename: Shu
authors.initials: S
authors.lastname: Ishikawa
authors.forename: Yoshikazu
authors.initials: Y
authors.lastname: Kawai
authors.forename: Konosuke
authors.initials: K
authors.lastname: Hiramatsu
authors.forename: Masayoshi
authors.initials: M
authors.lastname: Kuwano
authors.forename: Naotake
authors.initials: N
authors.lastname: Ogasawara
mesh_terms: D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*; D001426:Bacterial Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D002455:Cell Division / Q000235:genetics*; D003598:Cytoskeletal Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D005816:Genetic Complementation Test; D047468:Immunoprecipitation; D013058:Mass Spectrometry; D008856:Microscopy, Fluorescence; D009154:Mutation; D020798:Two-Hybrid System Techniques
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C065103:FtsA protein, Bacteria; C071525:FtsZ protein, Bacteria