dc.creatorBordenave, César Daniel
dc.creatorGranados Mendoza, Carolina
dc.creatorJiménez Bremont, Juan Francisco
dc.creatorGárriz, Andrés
dc.creatorRodriguez, Andres Alberto
dc.date.accessioned2020-10-30T18:18:32Z
dc.date.accessioned2022-10-15T09:48:29Z
dc.date.available2020-10-30T18:18:32Z
dc.date.available2022-10-15T09:48:29Z
dc.date.created2020-10-30T18:18:32Z
dc.date.issued2019-01
dc.identifierBordenave, César Daniel; Granados Mendoza, Carolina; Jiménez Bremont, Juan Francisco; Gárriz, Andrés; Rodriguez, Andres Alberto; Defining novel plant polyamine oxidase subfamilies through molecular modeling and sequence analysis; BioMed Central; BMC Evolutionary Biology; 19; 1; 1-2019; 1-15
dc.identifier1471-2148
dc.identifierhttp://hdl.handle.net/11336/117286
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4372272
dc.description.abstractBackground: The polyamine oxidases (PAOs) catabolize the oxidative deamination of the polyamines (PAs) spermine (Spm) and spermidine (Spd). Most of the phylogenetic studies performed to analyze the plant PAO family took into account only a limited number and/or taxonomic representation of plant PAOs sequences. Results: Here, we constructed a plant PAO protein sequence database and identified four subfamilies. Subfamily PAO back conversion 1 (PAObc1) was present on every lineage included in these analyses, suggesting that BC-type PAOs might play an important role in plants, despite its precise function is unknown. Subfamily PAObc2 was exclusively present in vascular plants, suggesting that t-Spm oxidase activity might play an important role in the development of the vascular system. The only terminal catabolism (TC) PAO subfamily (subfamily PAOtc) was lost in Superasterids but it was present in all other land plants. This indicated that the TC-type reactions are fundamental for land plants and that their function could being taken over by other enzymes in Superasterids. Subfamily PAObc3 was the result of a gene duplication event preceding Angiosperm diversification, followed by a gene extinction in Monocots. Differential conserved protein motifs were found for each subfamily of plant PAOs. The automatic assignment using these motifs was found to be comparable to the assignment by rough clustering performed on this work. Conclusions: The results presented in this work revealed that plant PAO family is bigger than previously conceived. Also, they delineate important background information for future specific structure-function and evolutionary investigations and lay a foundation for the deeper characterization of each plant PAO subfamily.
dc.languageeng
dc.publisherBioMed Central
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://bmcevolbiol.biomedcentral.com/articles/10.1186/s12862-019-1361-z
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1186/s12862-019-1361-z
dc.rightshttps://creativecommons.org/licenses/by/2.5/ar/
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectEVOLUTION
dc.subjectHOMOLOGY MODELING
dc.subjectPHYLOGENY
dc.subjectPOLYAMINE CATABOLISM
dc.subjectPOLYAMINE OXIDASE
dc.subjectPROTEIN STRUCTURE
dc.titleDefining novel plant polyamine oxidase subfamilies through molecular modeling and sequence analysis
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


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