title: ZipN, an FtsA-like orchestrator of divisome assembly in the model cyanobacterium Synechocystis PCC6803.
abstract: We pursued the characterization of the divisome of the spherical-celled cyanobacterium Synechocystis PCC6803, through deletion, site-directed mutagenesis, GFP tagging, two-hybrid and co-immunoprecipitation assays. We presently report that the DivIVA-like protein Cdv3 is essential to both cell growth and division, whereas the AmiC, AmpH, FtsE, FtsN, SpoIID, YlmD, YlmE and YlmG proteins are dispensable. With the exception of the self-interacting protein YlmD, none of these dispensable factors appeared to interact with ZipN, the crucial cytokinetic factor we previously characterized. By contrast, we found that ZipN interacts with itself and the self-interacting protein Cdv3, as well as with all other crucial cytokinetic factors we previously characterized, namely: FtsZ, FtsI, FtsQ, SepF and ZipS. We also identified ZipN amino acids selectively involved in ZipN interaction with one of its following partners, Cdv3, FtsQ or SepF. Finally, we found no direct interaction between Cdv3, SepF and ZipS. Collectively, these results indicate that ZipN is a central player of divisome assembly in cyanobacteria, similarly to the FtsA protein of E. coli that is absent in cyanobacteria and chloroplast.
authors.affiliation: CEA, iBiTec-S, SBIGeM, LBI, Bat 142 CEA-Saclay, F-91191 Gif sur Yvette Cedex, France.
authors.forename: Martial
authors.initials: M
authors.lastname: Marbouty
authors.forename: Cyril
authors.initials: C
authors.lastname: Saguez
authors.forename: Corinne
authors.initials: C
authors.lastname: Cassier-Chauvat
authors.forename: Franck
authors.initials: F
authors.lastname: Chauvat
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D048749:Cytokinesis; D047468:Immunoprecipitation; D050296:Microbial Viability; D016297:Mutagenesis, Site-Directed; D025941:Protein Interaction Mapping; D046939:Synechocystis / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins