Gene Coexpression Analysis Reveals Complex Metabolism of the Monoterpene Alcohol Linalool in<i>Arabidopsis</i>Flowers
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- Jean-François Ginglinger
- Institute of Plant Molecular Biology, Centre National de la Recherche Scientifique Unité Propre de Recherche 2357, University of Strasbourg, F-67000 Strasbourg, France
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- Benoit Boachon
- Institute of Plant Molecular Biology, Centre National de la Recherche Scientifique Unité Propre de Recherche 2357, University of Strasbourg, F-67000 Strasbourg, France
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- René Höfer
- Institute of Plant Molecular Biology, Centre National de la Recherche Scientifique Unité Propre de Recherche 2357, University of Strasbourg, F-67000 Strasbourg, France
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- Christian Paetz
- Max Planck Institute for Chemical Ecology, D-07745 Jena, Germany
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- Tobias G. Köllner
- Max Planck Institute for Chemical Ecology, D-07745 Jena, Germany
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- Laurence Miesch
- Laboratoire de Chimie Organique Synthétique, Centre National de la Recherche Scientifique Unité Mixte de Recherche 7177, University of Strasbourg, France
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- Raphael Lugan
- Institute of Plant Molecular Biology, Centre National de la Recherche Scientifique Unité Propre de Recherche 2357, University of Strasbourg, F-67000 Strasbourg, France
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- Raymonde Baltenweck
- Laboratoire Métabolisme Secondaire de la Vigne, Institut National de la Recherche Agronomique Unité Mixte de Recherche 1131, University of Strasbourg, Colmar, F-68021 France
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- Jérôme Mutterer
- Institute of Plant Molecular Biology, Centre National de la Recherche Scientifique Unité Propre de Recherche 2357, University of Strasbourg, F-67000 Strasbourg, France
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- Pascaline Ullmann
- Institute of Plant Molecular Biology, Centre National de la Recherche Scientifique Unité Propre de Recherche 2357, University of Strasbourg, F-67000 Strasbourg, France
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- Franziska Beran
- Max Planck Institute for Chemical Ecology, D-07745 Jena, Germany
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- Patricia Claudel
- Laboratoire Métabolisme Secondaire de la Vigne, Institut National de la Recherche Agronomique Unité Mixte de Recherche 1131, University of Strasbourg, Colmar, F-68021 France
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- Francel Verstappen
- Laboratory of Plant Physiology, Wageningen University, 6700 AR Wageningen, The Netherlands
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- Marc J.C. Fischer
- Laboratoire Métabolisme Secondaire de la Vigne, Institut National de la Recherche Agronomique Unité Mixte de Recherche 1131, University of Strasbourg, Colmar, F-68021 France
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- Francis Karst
- Laboratoire Métabolisme Secondaire de la Vigne, Institut National de la Recherche Agronomique Unité Mixte de Recherche 1131, University of Strasbourg, Colmar, F-68021 France
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- Harro Bouwmeester
- Laboratory of Plant Physiology, Wageningen University, 6700 AR Wageningen, The Netherlands
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- Michel Miesch
- Laboratoire de Chimie Organique Synthétique, Centre National de la Recherche Scientifique Unité Mixte de Recherche 7177, University of Strasbourg, France
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- Bernd Schneider
- Max Planck Institute for Chemical Ecology, D-07745 Jena, Germany
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- Jonathan Gershenzon
- Max Planck Institute for Chemical Ecology, D-07745 Jena, Germany
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- Jürgen Ehlting
- Department of Biology, Centre for Forest Biology, University of Victoria, Victoria, British Columbia V8P 5C2, Canada
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- Danièle Werck-Reichhart
- Institute of Plant Molecular Biology, Centre National de la Recherche Scientifique Unité Propre de Recherche 2357, University of Strasbourg, F-67000 Strasbourg, France
抄録
<jats:title>Abstract</jats:title><jats:p>The cytochrome P450 family encompasses the largest family of enzymes in plant metabolism, and the functions of many of its members in Arabidopsis thaliana are still unknown. Gene coexpression analysis pointed to two P450s that were coexpressed with two monoterpene synthases in flowers and were thus predicted to be involved in monoterpenoid metabolism. We show that all four selected genes, the two terpene synthases (TPS10 and TPS14) and the two cytochrome P450s (CYP71B31 and CYP76C3), are simultaneously expressed at anthesis, mainly in upper anther filaments and in petals. Upon transient expression in Nicotiana benthamiana, the TPS enzymes colocalize in vesicular structures associated with the plastid surface, whereas the P450 proteins were detected in the endoplasmic reticulum. Whether they were expressed in Saccharomyces cerevisiae or in N. benthamiana, the TPS enzymes formed two different enantiomers of linalool: (−)-(R)-linalool for TPS10 and (+)-(S)-linalool for TPS14. Both P450 enzymes metabolize the two linalool enantiomers to form different but overlapping sets of hydroxylated or epoxidized products. These oxygenated products are not emitted into the floral headspace, but accumulate in floral tissues as further converted or conjugated metabolites. This work reveals complex linalool metabolism in Arabidopsis flowers, the ecological role of which remains to be determined.</jats:p>
収録刊行物
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- The Plant Cell
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The Plant Cell 25 (11), 4640-4657, 2013-11-01
Oxford University Press (OUP)
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詳細情報 詳細情報について
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- CRID
- 1363670319984552832
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- ISSN
- 1532298X
- 10404651
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- データソース種別
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- Crossref