ArticleThe Plant cell2013
Evolution of homospermidine synthase in the convolvulaceae: a story of gene duplication, gene loss, and periods of various selection pressures.
Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 43 citations in OpenAlex.
- Roots of Indian heliotrope (Heliotropium indicum) produce simple pyrrolizidine alkaloids using the same homospermidine oxidase involved in biosynthesis of complex pyrrolizidine alkaloids in aerial parts.Plant biology (Stuttgart, Germany) · 2025Article
- Homospermidine synthase evolution and the origin(s) of pyrrolizidine alkaloids in Apocynaceae.American journal of botany · 2025Article
- Seeing double: two different homospermidine oxidases are involved in pyrrolizidine alkaloid biosynthesis in different organs of comfrey (Symphytum officinale).The Plant journal : for cell and molecular biology · 2024Article
- Pyrrolizidine alkaloids are synthesized and accumulated in flower of Myosotis scorpioides.Journal of plant research · 2024Article
- Mutational biases favor complexity increases in protein interaction networks after gene duplication.Molecular systems biology · 2024Article
- Detection and Quantification of Botanical Impurities in Commercial Oregano (Foods (Basel, Switzerland) · 2023Article
- Genome-Wide Characterization of the PIFs Family in Sweet Potato and Functional Identification ofInternational journal of molecular sciences · 2023Article
- The long road of functional recruitment-The evolution of a gene duplicate to pyrrolizidine alkaloid biosynthesis in the morning glories (Convolvulaceae).Plant direct · 2022Article
- Insights into polyamine metabolism: homospermidine is double-oxidized in two discrete steps by a single copper-containing amine oxidase in pyrrolizidine alkaloid biosynthesis.The Plant cell · 2022Article
- A Collaborative Classroom Investigation of the Evolution of SABATH Methyltransferase Substrate Preference Shifts over 120 My of Flowering Plant History.Molecular biology and evolution · 2022Article
- CRISPR/Cas9-Mediated Genome Editing in Comfrey (Molecules (Basel, Switzerland) · 2021Article
- Development of an activity assay for characterizing deoxyhypusine synthase and its diverse reaction products.FEBS open bio · 2021Article
- The evolution of metabolism: How to test evolutionary hypotheses at the genomic level.Computational and structural biotechnology journal · 2020Review
- Metabolic diversification of nitrogen-containing metabolites by the expression of a heterologous lysine decarboxylase gene in Arabidopsis.The Plant journal : for cell and molecular biology · 2019Article
- Specific Distribution of Pyrrolizidine Alkaloids in Floral Parts of Comfrey (Symphytum officinale) and its Implications for Flower Ecology.Journal of chemical ecology · 2019Article
- Low pyrrolizidine alkaloid levels in perennial ryegrass is associated with the absence of a homospermidine synthase gene.BMC plant biology · 2018Article
- Evolution of pyrrolizidine alkaloid biosynthesis in Apocynaceae: revisiting the defence de-escalation hypothesis.The New phytologist · 2018Article
- Article
- Identification of a Second Site of Pyrrolizidine Alkaloid Biosynthesis in Comfrey to Boost Plant Defense in Floral StagePlant physiology · 2017Article
- Molecular Evolution and Functional Characterization of a Bifunctional Decarboxylase Involved in Lycopodium Alkaloid Biosynthesis.Plant physiology · 2016Article
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3 authors at 2 institutions in 1 country.
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Abstract
Homospermidine synthase (HSS), the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, is known to have its origin in the duplication of a gene encoding deoxyhypusine synthase. To study the processes that followed this gene duplication event and gave rise to HSS, we identified sequences encoding HSS and deoxyhypusine synthase from various species of the Convolvulaceae. We show that HSS evolved only once in this lineage. This duplication event was followed by several losses of a functional gene copy attributable to gene loss or pseudogenization. Statistical analyses of sequence data suggest that, in those lineages in which the gene copy was successfully recruited as HSS, the gene duplication event was followed by phases of various selection pressures, including purifying selection, relaxed functional constraints, and possibly positive Darwinian selection. Site-specific mutagenesis experiments have confirmed that the substitution of sites predicted to be under positive Darwinian selection is sufficient to convert a deoxyhypusine synthase into a HSS. In addition, analyses of transcript levels have shown that HSS and deoxyhypusine synthase have also diverged with respect to their regulation. The impact of protein-protein interaction on the evolution of HSS is discussed with respect to current models of enzyme evolution.
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