In Planta Recapitulation of Isoprene Synthase Evolution from Ocimene Synthases
| Autor: | Claudio Varotto, Urska Vrhovsek, Alberto Algarra Alarcon, Enrico Barbaro, Francesco Loreto, Jia Xu, Mingai Li, Luca Cappellin, Violeta Velikova, Silvia Carlin |
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| Přispěvatelé: | Li, M, J, Xu, A Algarra, Alarcon, S, Carlin, E, Barbaro, L, Cappellin, V, Velikova, U, Vrhovsek, Loreto, F, C, Varotto |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0106 biological sciences
0301 basic medicine substrate specificity Monoterpene Arabidopsis Isoprene synthase 01 natural sciences Terpene Ocimene Evolution Molecular 03 medical and health sciences chemistry.chemical_compound Hemiterpenes Pentanes short-chain terpene synthases parallel evolution Genetics Isoprene synthase evolution Short-chain terpene synthases parallel evolution Site-directed mutagenesis Substrate specificity Active site size modulation Ocimene synthase Butadienes Amino Acid Sequence Molecular Biology Ecology Evolution Behavior and Systematics Isoprene Discoveries Plant Proteins Alkyl and Aryl Transferases biology Sequence Homology Amino Acid active site size modulation Settore BIO/02 - BOTANICA SISTEMATICA ocimene synthase 15. Life on land biology.organism_classification 030104 developmental biology chemistry Biochemistry biology.protein Mutagenesis Site-Directed Neofunctionalization site-directed mutagenesis Function (biology) isoprene synthase evolution 010606 plant biology & botany |
| Zdroj: | Molecular Biology and Evolution |
| ISSN: | 1537-1719 0737-4038 |
| Popis: | Isoprene is the most abundant biogenic volatile hydrocarbon compound naturally emitted by plants and plays a major role in atmospheric chemistry. It has been proposed that isoprene synthases (IspS) may readily evolve from other terpene synthases, but this hypothesis has not been experimentally investigated. We isolated and functionally validated in Arabidopsis the first isoprene synthase gene, AdoIspS, from a monocotyledonous species (Arundo donax L., Poaceae). Phylogenetic reconstruction indicates that AdoIspS and dicots isoprene synthases most likely originated by parallel evolution from TPS-b monoterpene synthases. Site-directed mutagenesis demonstrated invivo the functional and evolutionary relevance of the residues considered diagnostic for IspS function. One of these positions was identified by saturating mutagenesis as a major determinant of substrate specificity in AdoIspS able to cause invivo a dramatic change in total volatile emission from hemi- to monoterpenes and supporting evolution of isoprene synthases from ocimene synthases. The mechanism responsible for IspS neofunctionalization by active site size modulation by a single amino acid mutation demonstrated in this study might be general, as the very same amino acidic position is implicated in the parallel evolution of different short-chain terpene synthases from both angiosperms and gymnosperms. Based on these results, we present a model reconciling in a unified conceptual framework the apparently contrasting patterns previously observed for isoprene synthase evolution in plants. These results indicate that parallel evolution may be driven by relatively simple biophysical constraints, and illustrate the intimate molecular evolutionary links between the structural and functional bases of traits with global relevance. |
| Databáze: | OpenAIRE |
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