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FtsZ of Filamentous, Heterocyst-Forming Cyanobacteria Has a Conserved N-Terminal Peptide Required for Normal FtsZ Polymerization and Cell Division

AuthorsCorrales-Guerrero, Laura CSIC ORCID; Camargo, Sergio CSIC ORCID ; Valladares, Ana CSIC ORCID; Picossi, Silvia CSIC ORCID ; Luque, Ignacio CSIC ORCID ; Ochoa de Alda, Jesús A.G.; Herrero, Antonia CSIC ORCID
KeywordsCell division
Cyanobacterial FtsZ phylogeny
ZipN phylogeny
Bacterial multicellularity
Issue Date2018
PublisherFrontiers Media
CitationFrontiers in Microbiology 9: 2260 (2018)
AbstractFilamentous cyanobacteria grow by intercalary cell division, which should involve distinct steps compared to those producing separate daughter cells. The N-terminal region of FtsZ is highly conserved in the clade of filamentous cyanobacteria capable of cell differentiation. A derivative of the model strain Anabaena sp. PCC 7120 expressing only an FtsZ lacking the amino acids 2¿51 of the N-terminal peptide (1N-FtsZ) could not be segregated. Strain CSL110 expresses both 1N-FtsZ, from the endogenous ftsZ gene promoter, and the native FtsZ from a synthetic regulated promoter. Under conditions of 1N-FtsZ predominance, cells of strain CSL110 progressively enlarge, reflecting reduced cell division, and show instances of asymmetric cell division and aberrant Z-structures notably differing from the Z-ring formed by FtsZ in the wild type. In bacterial 2-hybrid assays FtsZ interacted with 1N-FtsZ. However, 1N-FtsZ-GFP appeared impaired for incorporation into Z-rings when expressed together with FtsZ. FtsZ, but not 1N-FtsZ, interacted with the essential protein SepF. Both FtsZ and 1N-FtsZ polymerize in vitro exhibiting comparable GTPase activities. However, filaments of FtsZ show a distinct curling forming toroids, whereas 1N-FtsZ form thick bundles of straight filaments. Thus, the N-terminal FtsZ sequence appears to contribute to a distinct FtsZ polymerization mode that is essential for cell division and division plane location in Anabaena.
Identifiersdoi: 10.3389/fmicb.2018.02260
issn: 1664-302X
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