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Biosynthesis and antifungal activity of fungus-induced O-methylated flavonoids in maize
Fungal infection of grasses, including rice (Oryza sativa), sorghum (Sorghum bicolor), and barley (Hordeum vulgare), induces the formation and accumulation of flavonoid phytoalexins. In maize (Zea mays), however, investigators have emphasized benzoxazinoid and terpenoid phytoalexins, and comparative...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8774720/ https://www.ncbi.nlm.nih.gov/pubmed/34718797 http://dx.doi.org/10.1093/plphys/kiab496 |
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author | Förster, Christiane Handrick, Vinzenz Ding, Yezhang Nakamura, Yoko Paetz, Christian Schneider, Bernd Castro-Falcón, Gabriel Hughes, Chambers C Luck, Katrin Poosapati, Sowmya Kunert, Grit Huffaker, Alisa Gershenzon, Jonathan Schmelz, Eric A Köllner, Tobias G |
author_facet | Förster, Christiane Handrick, Vinzenz Ding, Yezhang Nakamura, Yoko Paetz, Christian Schneider, Bernd Castro-Falcón, Gabriel Hughes, Chambers C Luck, Katrin Poosapati, Sowmya Kunert, Grit Huffaker, Alisa Gershenzon, Jonathan Schmelz, Eric A Köllner, Tobias G |
author_sort | Förster, Christiane |
collection | PubMed |
description | Fungal infection of grasses, including rice (Oryza sativa), sorghum (Sorghum bicolor), and barley (Hordeum vulgare), induces the formation and accumulation of flavonoid phytoalexins. In maize (Zea mays), however, investigators have emphasized benzoxazinoid and terpenoid phytoalexins, and comparatively little is known about flavonoid induction in response to pathogens. Here, we examined fungus-elicited flavonoid metabolism in maize and identified key biosynthetic enzymes involved in the formation of O-methylflavonoids. The predominant end products were identified as two tautomers of a 2-hydroxynaringenin-derived compound termed xilonenin, which significantly inhibited the growth of two maize pathogens, Fusarium graminearum and Fusarium verticillioides. Among the biosynthetic enzymes identified were two O-methyltransferases (OMTs), flavonoid OMT 2 (FOMT2), and FOMT4, which demonstrated distinct regiospecificity on a broad spectrum of flavonoid classes. In addition, a cytochrome P450 monooxygenase (CYP) in the CYP93G subfamily was found to serve as a flavanone 2-hydroxylase providing the substrate for FOMT2-catalyzed formation of xilonenin. In summary, maize produces a diverse blend of O-methylflavonoids with antifungal activity upon attack by a broad range of fungi. |
format | Online Article Text |
id | pubmed-8774720 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-87747202022-01-21 Biosynthesis and antifungal activity of fungus-induced O-methylated flavonoids in maize Förster, Christiane Handrick, Vinzenz Ding, Yezhang Nakamura, Yoko Paetz, Christian Schneider, Bernd Castro-Falcón, Gabriel Hughes, Chambers C Luck, Katrin Poosapati, Sowmya Kunert, Grit Huffaker, Alisa Gershenzon, Jonathan Schmelz, Eric A Köllner, Tobias G Plant Physiol Research Articles Fungal infection of grasses, including rice (Oryza sativa), sorghum (Sorghum bicolor), and barley (Hordeum vulgare), induces the formation and accumulation of flavonoid phytoalexins. In maize (Zea mays), however, investigators have emphasized benzoxazinoid and terpenoid phytoalexins, and comparatively little is known about flavonoid induction in response to pathogens. Here, we examined fungus-elicited flavonoid metabolism in maize and identified key biosynthetic enzymes involved in the formation of O-methylflavonoids. The predominant end products were identified as two tautomers of a 2-hydroxynaringenin-derived compound termed xilonenin, which significantly inhibited the growth of two maize pathogens, Fusarium graminearum and Fusarium verticillioides. Among the biosynthetic enzymes identified were two O-methyltransferases (OMTs), flavonoid OMT 2 (FOMT2), and FOMT4, which demonstrated distinct regiospecificity on a broad spectrum of flavonoid classes. In addition, a cytochrome P450 monooxygenase (CYP) in the CYP93G subfamily was found to serve as a flavanone 2-hydroxylase providing the substrate for FOMT2-catalyzed formation of xilonenin. In summary, maize produces a diverse blend of O-methylflavonoids with antifungal activity upon attack by a broad range of fungi. Oxford University Press 2021-10-27 /pmc/articles/PMC8774720/ /pubmed/34718797 http://dx.doi.org/10.1093/plphys/kiab496 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of American Society of Plant Biologists. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Förster, Christiane Handrick, Vinzenz Ding, Yezhang Nakamura, Yoko Paetz, Christian Schneider, Bernd Castro-Falcón, Gabriel Hughes, Chambers C Luck, Katrin Poosapati, Sowmya Kunert, Grit Huffaker, Alisa Gershenzon, Jonathan Schmelz, Eric A Köllner, Tobias G Biosynthesis and antifungal activity of fungus-induced O-methylated flavonoids in maize |
title | Biosynthesis and antifungal activity of fungus-induced O-methylated flavonoids in maize |
title_full | Biosynthesis and antifungal activity of fungus-induced O-methylated flavonoids in maize |
title_fullStr | Biosynthesis and antifungal activity of fungus-induced O-methylated flavonoids in maize |
title_full_unstemmed | Biosynthesis and antifungal activity of fungus-induced O-methylated flavonoids in maize |
title_short | Biosynthesis and antifungal activity of fungus-induced O-methylated flavonoids in maize |
title_sort | biosynthesis and antifungal activity of fungus-induced o-methylated flavonoids in maize |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8774720/ https://www.ncbi.nlm.nih.gov/pubmed/34718797 http://dx.doi.org/10.1093/plphys/kiab496 |
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