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Zipor, G., Department of Ornamental Horticulture, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Duarte, P., IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre, 823, Porto, Portugal
Carqueijeiro, I., IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre, 823, Porto, Portugal
Shahar, L., Department of Ornamental Horticulture, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Ovadia, R., Department of Ornamental Horticulture, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Teper-Bamnolker, P., Department of Postharvest Science of Fresh Produce, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Eshel, D., Department of Postharvest Science of Fresh Produce, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Levin, Y., The Nancy and Stephen Grand Israel National Center, Personalized Medicine Weizmann Institute of Science, Rehovot, Israel
Doron-Faigenboim, A., Department of Fruit Tree Science, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Sottomayor, M., IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre, 823, Porto, Portugal, Departamento de Biologia, Faculdade de Ciências da Universidade do Porto, Rua do Campo Alegre s/n 4169-007, Porto, Portugal
Oren-Shamir, M., Department of Ornamental Horticulture, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Summary: In contrast to detailed knowledge regarding the biosynthesis of anthocyanins, the largest group of plant pigments, little is known about their in planta degradation. It has been suggested that anthocyanin degradation is enzymatically controlled and induced when beneficial to the plant. Here we investigated the enzymatic process in Brunfelsia calycina flowers, as they changed color from purple to white. We characterized the enzymatic process by which B. calycina protein extracts degrade anthocyanins. A candidate peroxidase was partially purified and characterized and its intracellular localization was determined. The transcript sequence of this peroxidase was fully identified. A basic peroxidase, BcPrx01, is responsible for the in planta degradation of anthocyanins in B. calycina flowers. BcPrx01 has the ability to degrade complex anthocyanins, it co-localizes with these pigments in the vacuoles of petals, and both the mRNA and protein levels of BcPrx01 are greatly induced parallel to the degradation of anthocyanins. Both isoelectric focusing (IEF) gel analysis and 3D structure prediction indicated that BcPrx01 is cationic. Identification of BcPrx01 is a significant breakthrough both in the understanding of anthocyanin catabolism in plants and in the field of peroxidases, where such a consistent relationship between expression levels, in planta subcellular localization and activity has seldom been demonstrated. © 2014 New Phytologist Trust.
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In planta anthocyanin degradation by a vacuolar class III peroxidase in Brunfelsia calycina flowers
205
Zipor, G., Department of Ornamental Horticulture, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Duarte, P., IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre, 823, Porto, Portugal
Carqueijeiro, I., IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre, 823, Porto, Portugal
Shahar, L., Department of Ornamental Horticulture, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Ovadia, R., Department of Ornamental Horticulture, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Teper-Bamnolker, P., Department of Postharvest Science of Fresh Produce, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Eshel, D., Department of Postharvest Science of Fresh Produce, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Levin, Y., The Nancy and Stephen Grand Israel National Center, Personalized Medicine Weizmann Institute of Science, Rehovot, Israel
Doron-Faigenboim, A., Department of Fruit Tree Science, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
Sottomayor, M., IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre, 823, Porto, Portugal, Departamento de Biologia, Faculdade de Ciências da Universidade do Porto, Rua do Campo Alegre s/n 4169-007, Porto, Portugal
Oren-Shamir, M., Department of Ornamental Horticulture, Agriculture Research Organization, The Volcani Center, PO Box 6 Beit Dagan 50250, Beit Dagan, Israel
In planta anthocyanin degradation by a vacuolar class III peroxidase in Brunfelsia calycina flowers
Summary: In contrast to detailed knowledge regarding the biosynthesis of anthocyanins, the largest group of plant pigments, little is known about their in planta degradation. It has been suggested that anthocyanin degradation is enzymatically controlled and induced when beneficial to the plant. Here we investigated the enzymatic process in Brunfelsia calycina flowers, as they changed color from purple to white. We characterized the enzymatic process by which B. calycina protein extracts degrade anthocyanins. A candidate peroxidase was partially purified and characterized and its intracellular localization was determined. The transcript sequence of this peroxidase was fully identified. A basic peroxidase, BcPrx01, is responsible for the in planta degradation of anthocyanins in B. calycina flowers. BcPrx01 has the ability to degrade complex anthocyanins, it co-localizes with these pigments in the vacuoles of petals, and both the mRNA and protein levels of BcPrx01 are greatly induced parallel to the degradation of anthocyanins. Both isoelectric focusing (IEF) gel analysis and 3D structure prediction indicated that BcPrx01 is cationic. Identification of BcPrx01 is a significant breakthrough both in the understanding of anthocyanin catabolism in plants and in the field of peroxidases, where such a consistent relationship between expression levels, in planta subcellular localization and activity has seldom been demonstrated. © 2014 New Phytologist Trust.
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