Abstract
Polyamine oxidases (PAOs) are characterized by a broad variability in catalytic properties and subcellular localization, and impact key cellular processes in diverse organisms. In the present study, a comprehensive phylogenetic analysis was performed to understand the evolution of PAOs across the three domains of life and particularly within eukaryotes. Phylogenetic trees show that PAO-like sequences of bacteria, archaea, and eukaryotes form three distinct clades, with the exception of a few procaryotes that probably acquired a PAO gene through horizontal transfer from a eukaryotic donor. Results strongly support a common origin for archaeal PAO-like proteins and eukaryotic PAOs, as well as a shared origin between PAOs and monoamine oxidases. Within eukaryotes, four main lineages were identified that likely originated from an ancestral eukaryotic PAO before the split of the main superphyla, followed by specific gene losses in each superphylum. Plant PAOs show the highest diversity within eukaryotes and belong to three distinct clades that underwent to multiple events of gene duplication and gene loss. Peptide deletion along the evolution of plant PAOs of Clade I accounted for further diversification of function and subcellular localization. This study provides a reference for future structure–function studies and emphasizes the importance of extending comparisons among PAO subfamilies across multiple eukaryotic superphyla.
Highlights
Polyamine oxidases (PAOs) are characterized by a broad variability in catalytic properties and subcellular localization, and impact key cellular processes in diverse organisms
Phylogenetic studies have suggested that the spermidine synthase (SPDS) genes of the various organisms derive from a common ancestor preceding the separation between prokaryotes and eukaryotes and that they have been the origin of spermine synthase (SPMS) and thermospermine synthase (TSPMS) activities through gene duplication and/or neofunctionalization[16]
Proteins of the Archaea clade are recovered as sister to the Eukaryota clade (BS = 100; Fig. 1) using either the midpoint or the Minimal Ancestor Deviation (MAD) rooting methods, suggesting a shared evolutionary history between archaeal PAO-like proteins and eukaryotic PAOs
Summary
Polyamine oxidases (PAOs) are characterized by a broad variability in catalytic properties and subcellular localization, and impact key cellular processes in diverse organisms. Phylogenetic studies have suggested that the SPDS genes of the various organisms derive from a common ancestor preceding the separation between prokaryotes and eukaryotes and that they have been the origin of SPMS and TSPMS activities through gene duplication and/or neofunctionalization[16]. PAOs are characterized by a broad variability in substrate specificity, catalytic mechanism and subcellular localization. They are FADdependent enzymes catalyzing the oxidation of the free, and/or acetylated form, of polyamines at the secondary amino g roups[19,20,21]. Unlike PAOXs and SMOXs, Saccharomyces cerevisiae PAO (FMS1) catalyzes the oxidation of both acetylated and non-acetylated p olyamines[25,26]
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