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FtsZ of filamentous, heterocyst-forming cyanobacteria has a conserved N-Terminal peptide required for normal FtsZ polymerization and cell division
dc.creator | Corrales Guerrero, Laura | es |
dc.creator | Camargo Bernal, Sergio | es |
dc.creator | Valladares Ruiz, Ana | es |
dc.creator | Picossi Goñi, Silvia María | es |
dc.creator | Luque Romero, Ignacio | es |
dc.creator | Ochoa de Alda, Jesús A. G. | es |
dc.creator | Herrero Moreno, Antonia | es |
dc.date.accessioned | 2019-03-21T10:49:39Z | |
dc.date.available | 2019-03-21T10:49:39Z | |
dc.date.issued | 2018-10-02 | |
dc.identifier.citation | Corrales Guerrero, L., Camargo Bernal, S., Valladares Ruiz, A., Picossi Goñi, S.M., Luque Romero, I., Ochoa de Alda, J.A.G. y Herrero Moreno, A. (2018). FtsZ of filamentous, heterocyst-forming cyanobacteria has a conserved N-Terminal peptide required for normal FtsZ polymerization and cell division. Frontiers in Microbiology, 9 (2260), 1-20. | |
dc.identifier.issn | 1664-302X | es |
dc.identifier.uri | https://hdl.handle.net/11441/84510 | |
dc.description.abstract | Filamentous 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. | es |
dc.description.sponsorship | Agencia Estatal de Investigación BFU2013-44686-P BFU2016-77097-P | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Frontiers Media | es |
dc.relation.ispartof | Frontiers in Microbiology, 9 (2260), 1-20. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Anabaena | es |
dc.subject | ZipN phylogeny | es |
dc.subject | Bacterial multicellularity | es |
dc.subject | Cell division | es |
dc.subject | Cyanobacterial FtsZ phylogeny | es |
dc.title | FtsZ of filamentous, heterocyst-forming cyanobacteria has a conserved N-Terminal peptide required for normal FtsZ polymerization and cell division | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular | es |
dc.relation.projectID | BFU2013-44686-P | es |
dc.relation.projectID | BFU2016-77097-P | es |
dc.relation.publisherversion | http://dx.doi.org/10.3389/fmicb.2018.02260 | es |
dc.identifier.doi | 10.3389/fmicb.2018.02260 | es |
idus.format.extent | 20 p. | es |
dc.journaltitle | Frontiers in Microbiology | es |
dc.publication.volumen | 9 | es |
dc.publication.issue | 2260 | es |
dc.publication.initialPage | 1 | es |
dc.publication.endPage | 20 | es |