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PYK10 myrosinase reveals a functional coordination between endoplasmic reticulum bodies and glucosinolates in <i>Arabidopsis thaliana</i>
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- Ryohei T. Nakano
- Department of Plant Microbe Interactions Max Planck Institute for Plant Breeding Research Carl‐von‐Linné‐Weg 10 D‐50829 Köln Germany
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- Mariola Piślewska‐Bednarek
- Institute of Bioorganic Chemistry Polish Academy of Sciences Noskowskiego 12/14 61‐704 Poznań Poland
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- Kenji Yamada
- Department of Cell Biology National Institute of Basic Biology Okazaki 444‐8585 Japan
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- Patrick P. Edger
- Department of Plant and Microbial Biology University of California Berkeley CA 94720 USA
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- Mado Miyahara
- Department of Botany Graduate School of Science Kyoto University Sakyo‐ku Kyoto 606‐8502 Japan
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- Maki Kondo
- Department of Cell Biology National Institute of Basic Biology Okazaki 444‐8585 Japan
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- Christoph Böttcher
- Department of Stress and Developmental Biology Leibniz Institute of Plant Biochemistry D‐06120 Halle (Saale) Germany
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- Masashi Mori
- Ishikawa Prefectural University Nonoichi Ishikawa 834‐1213 Japan
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- Mikio Nishimura
- Department of Cell Biology National Institute of Basic Biology Okazaki 444‐8585 Japan
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- Paul Schulze‐Lefert
- Department of Plant Microbe Interactions Max Planck Institute for Plant Breeding Research Carl‐von‐Linné‐Weg 10 D‐50829 Köln Germany
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- Ikuko Hara‐Nishimura
- Department of Botany Graduate School of Science Kyoto University Sakyo‐ku Kyoto 606‐8502 Japan
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- Paweł Bednarek
- Institute of Bioorganic Chemistry Polish Academy of Sciences Noskowskiego 12/14 61‐704 Poznań Poland
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Description
<jats:title>Summary</jats:title><jats:p>The endoplasmic reticulum body (ER body) is an organelle derived from the ER that occurs in only three families of the order Brassicales and is suggested to be involved in plant defense. ER bodies in <jats:italic>Arabidopsis thaliana</jats:italic> contain large amounts of β‐glucosidases, but the physiological functions of ER bodies and these enzymes remain largely unclear. Here we show that PYK10, the most abundant β‐glucosidase in <jats:italic>A. thaliana</jats:italic> root ER bodies, hydrolyzes indole glucosinolates (IGs) in addition to the previously reported <jats:italic>in vitro</jats:italic> substrate scopolin. We found a striking co‐expression between ER body‐related genes (including <jats:italic>PYK10</jats:italic>), glucosinolate biosynthetic genes and the genes for so‐called specifier proteins affecting the terminal products of myrosinase‐mediated glucosinolate metabolism, indicating that these systems have been integrated into a common transcriptional network. Consistent with this, comparative metabolite profiling utilizing a number of <jats:italic>A. thaliana</jats:italic> relatives within Brassicaceae identified a clear phylogenetic co‐occurrence between ER bodies and IGs, but not between ER bodies and scopolin. Collectively, our findings suggest a functional link between ER bodies and glucosinolate metabolism <jats:italic>in planta</jats:italic>. In addition, <jats:italic>in silico</jats:italic> three‐dimensional modeling, combined with phylogenomic analysis, suggests that PYK10 represents a clade of 16 myrosinases that arose independently from the other well‐documented class of six thioglucoside glucohydrolases. These findings provide deeper insights into how glucosinolates are metabolized in cruciferous plants and reveal variation of the myrosinase–glucosinolate system within individual plants.</jats:p>
Journal
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- The Plant Journal
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The Plant Journal 89 (2), 204-220, 2016-12-19
Wiley
