A tomato tocopherol-binding protein sheds light on intracellular a-tocopherol metabolism in plants
Tocopherols are non-polar compounds synthesized in the plastids, which function as major antioxidants of the plant cells and are essential in the human diet. Both the intermediates and final products of the tocopherol biosynthetic pathway must cross plastid membranes to reach their sites of action. So far, no protein with tocopherol binding activity has been reported in plants. Here, we demonstrated that the tomato SlTBP protein is targeted to chloroplasts and able to bind α-tocopherol. SlTBP-knockdown tomato plants exhibited reduced levels of tocopherol in both leaves and fruits. Several tocopherol deficiency phenotypes were apparent in the transgenic lines, such as alterations in photosynthetic parameters, dramatic distortion of thylakoid membranes and significant variations in the lipid profile. These results, along with the altered expression of genes related to photosynthesis, and tetrapyrrole, lipid, isoprenoid, inositol/phosphoinositide and redox metabolism, suggest that SlTBP may act in conducting tocopherol (or its biosynthetic intermediates) between the plastid compartments and/or at the interface between chloroplast and endoplasmic reticulum membranes, affecting interorganellar lipid metabolism.
Main Authors: | , , , , , , , , , , , , , , , , , , , , , , , |
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Format: | info:ar-repo/semantics/artículo biblioteca |
Language: | eng |
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Oxford University Press
2018-11
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Subjects: | Tomatoes, Tocopherols, Chloroplasts, Proteins, Tomate, Tocoferoles, Cloroplasto, Proteínas, |
Online Access: | https://academic.oup.com/pcp/article/59/11/2188/5101312 http://hdl.handle.net/20.500.12123/4819 https://doi.org/10.1093/pcp/pcy191 |
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Tomatoes Tocopherols Chloroplasts Proteins Tomate Tocoferoles Cloroplasto Proteínas Tomatoes Tocopherols Chloroplasts Proteins Tomate Tocoferoles Cloroplasto Proteínas |
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Tomatoes Tocopherols Chloroplasts Proteins Tomate Tocoferoles Cloroplasto Proteínas Tomatoes Tocopherols Chloroplasts Proteins Tomate Tocoferoles Cloroplasto Proteínas Bermudez Salazar, Luisa del Pozo, Talía Lira, Bruno Silvestre Godoy, Fabiana de Boos, Irene Romano, Cecilia Previtali, Viola Almeida, Juliana Brehelin, Claire Asis, Ramón Quadrana, Leandro Daniel Demarco, Diego Alseekh, Saleh Salinas Gamboa, Rigel Perez-Flores, Laura Dominguez, Pia Guadalupe Rothan, Christophe Fernie, Alisdair R. Gonzalez, Maurıcio Stocker, Achim Hemmerle, Andreas Clausen, Mads Hartving Carrari, Fernando Rossi, Magdalena A tomato tocopherol-binding protein sheds light on intracellular a-tocopherol metabolism in plants |
description |
Tocopherols are non-polar compounds synthesized in the plastids, which function as major antioxidants of the plant cells and are essential in the human diet. Both the intermediates and final products of the tocopherol biosynthetic pathway must cross plastid membranes to reach their sites of action. So far, no protein with tocopherol binding activity has been reported in plants. Here, we demonstrated that the tomato SlTBP protein is targeted to chloroplasts and able to bind α-tocopherol. SlTBP-knockdown tomato plants exhibited reduced levels of tocopherol in both leaves and fruits. Several tocopherol deficiency phenotypes were apparent in the transgenic lines, such as alterations in photosynthetic parameters, dramatic distortion of thylakoid membranes and significant variations in the lipid profile. These results, along with the altered expression of genes related to photosynthesis, and tetrapyrrole, lipid, isoprenoid, inositol/phosphoinositide and redox metabolism, suggest that SlTBP may act in conducting tocopherol (or its biosynthetic intermediates) between the plastid compartments and/or at the interface between chloroplast and endoplasmic reticulum membranes, affecting interorganellar lipid metabolism. |
format |
info:ar-repo/semantics/artículo |
topic_facet |
Tomatoes Tocopherols Chloroplasts Proteins Tomate Tocoferoles Cloroplasto Proteínas |
author |
Bermudez Salazar, Luisa del Pozo, Talía Lira, Bruno Silvestre Godoy, Fabiana de Boos, Irene Romano, Cecilia Previtali, Viola Almeida, Juliana Brehelin, Claire Asis, Ramón Quadrana, Leandro Daniel Demarco, Diego Alseekh, Saleh Salinas Gamboa, Rigel Perez-Flores, Laura Dominguez, Pia Guadalupe Rothan, Christophe Fernie, Alisdair R. Gonzalez, Maurıcio Stocker, Achim Hemmerle, Andreas Clausen, Mads Hartving Carrari, Fernando Rossi, Magdalena |
author_facet |
Bermudez Salazar, Luisa del Pozo, Talía Lira, Bruno Silvestre Godoy, Fabiana de Boos, Irene Romano, Cecilia Previtali, Viola Almeida, Juliana Brehelin, Claire Asis, Ramón Quadrana, Leandro Daniel Demarco, Diego Alseekh, Saleh Salinas Gamboa, Rigel Perez-Flores, Laura Dominguez, Pia Guadalupe Rothan, Christophe Fernie, Alisdair R. Gonzalez, Maurıcio Stocker, Achim Hemmerle, Andreas Clausen, Mads Hartving Carrari, Fernando Rossi, Magdalena |
author_sort |
Bermudez Salazar, Luisa |
title |
A tomato tocopherol-binding protein sheds light on intracellular a-tocopherol metabolism in plants |
title_short |
A tomato tocopherol-binding protein sheds light on intracellular a-tocopherol metabolism in plants |
title_full |
A tomato tocopherol-binding protein sheds light on intracellular a-tocopherol metabolism in plants |
title_fullStr |
A tomato tocopherol-binding protein sheds light on intracellular a-tocopherol metabolism in plants |
title_full_unstemmed |
A tomato tocopherol-binding protein sheds light on intracellular a-tocopherol metabolism in plants |
title_sort |
tomato tocopherol-binding protein sheds light on intracellular a-tocopherol metabolism in plants |
publisher |
Oxford University Press |
publishDate |
2018-11 |
url |
https://academic.oup.com/pcp/article/59/11/2188/5101312 http://hdl.handle.net/20.500.12123/4819 https://doi.org/10.1093/pcp/pcy191 |
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oai:localhost:20.500.12123-48192019-04-04T17:15:00Z A tomato tocopherol-binding protein sheds light on intracellular a-tocopherol metabolism in plants Bermudez Salazar, Luisa del Pozo, Talía Lira, Bruno Silvestre Godoy, Fabiana de Boos, Irene Romano, Cecilia Previtali, Viola Almeida, Juliana Brehelin, Claire Asis, Ramón Quadrana, Leandro Daniel Demarco, Diego Alseekh, Saleh Salinas Gamboa, Rigel Perez-Flores, Laura Dominguez, Pia Guadalupe Rothan, Christophe Fernie, Alisdair R. Gonzalez, Maurıcio Stocker, Achim Hemmerle, Andreas Clausen, Mads Hartving Carrari, Fernando Rossi, Magdalena Tomatoes Tocopherols Chloroplasts Proteins Tomate Tocoferoles Cloroplasto Proteínas Tocopherols are non-polar compounds synthesized in the plastids, which function as major antioxidants of the plant cells and are essential in the human diet. Both the intermediates and final products of the tocopherol biosynthetic pathway must cross plastid membranes to reach their sites of action. So far, no protein with tocopherol binding activity has been reported in plants. Here, we demonstrated that the tomato SlTBP protein is targeted to chloroplasts and able to bind α-tocopherol. SlTBP-knockdown tomato plants exhibited reduced levels of tocopherol in both leaves and fruits. Several tocopherol deficiency phenotypes were apparent in the transgenic lines, such as alterations in photosynthetic parameters, dramatic distortion of thylakoid membranes and significant variations in the lipid profile. These results, along with the altered expression of genes related to photosynthesis, and tetrapyrrole, lipid, isoprenoid, inositol/phosphoinositide and redox metabolism, suggest that SlTBP may act in conducting tocopherol (or its biosynthetic intermediates) between the plastid compartments and/or at the interface between chloroplast and endoplasmic reticulum membranes, affecting interorganellar lipid metabolism. Instituto de Biotecnología Fil: Bermudez Salazar, Luisa. Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Lira, Bruno Silvestre. Universidade de São Pablo. Departamento de Botânica. Instituto de Biociencias; Brasil Fil: Godoy, Fabiana de. Universidade de São Pablo. Departamento de Botânica. Instituto de Biociencias; Brasil Fil: Boos, Irene. Technical University of Denmark. Center for Nanomedicine and Theranostics. Department of Chemistry; Dinamarca Fil: Romano, Cecilia. Technical University of Denmark. Center for Nanomedicine and Theranostics. Department of Chemistry; Dinamarca Fil: Previtali, Viola. Technical University of Denmark. Center for Nanomedicine and Theranostics. Department of Chemistry; Dinamarca Fil: Almeida, Juliana. Universidade de São Pablo. Departamento de Botânica. Instituto de Biociencias; Brasil Fil: Brehelin, Claire. Centre National de la Recherche Scientifique. Laboratory of Membrane Biogenesis; Francia Fil: Asis, Ramón. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas; Argentina Fil: Quadrana, Leandro Daniel. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina Fil: Demarco, Diego. Universidade de São Pablo. Departamento de Botânica. Instituto de Biociencias; Brasil Fil: Alseekh, Saleh. Max Planck Institute of Molecular Plant Physiology; Alemania Fil: Salinas Gamboa, Rigel. Universidad Autónoma Metropolitana. Laboratorio de Fisiología, Bioquímica y Biología Molecular de Plantas. Departamento de Ciencias de la Salud; México Fil: Perez-Flores, Laura. Universidad Autónoma Metropolitana. Laboratorio de Fisiología, Bioquímica y Biología Molecular de Plantas. Departamento de Ciencias de la Salud; México Fil: Dominguez, Pia Guadalupe. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Rothan, Christophe. Institut National de la Recherche Agronomique. Fruit Biology and Pathology Unit; Francia Fil: Fernie, Alisdair R. Max Planck Institute of Molecular Plant Physiology; Alemania Fil: Gonzalez, Maurıcio. Universidad de Chile. Laboratorio de Genética Molecular Vegetal; Chile Fil: Stocker, Achim. University of Berne. Department of Chemistry and Biochemistry; Suiza Fil: Hemmerle, Andreas. University of Berne. Department of Chemistry and Biochemistry; Suiza Fil: Clausen, Mads Hartving. Technical University of Denmark. Center for Nanomedicine and Theranostics. Department of Chemistry; Dinamarca Fil: Carrari, Fernando. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Universidade de São Pablo. Departamento de Botânica. Instituto de Biociencias; Brasil Fil: Rossi, Magdalena. Universidade de São Pablo. Departamento de Botânica. Instituto de Biociencias; Brasil 2019-04-04T17:08:20Z 2019-04-04T17:08:20Z 2018-11 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion https://academic.oup.com/pcp/article/59/11/2188/5101312 http://hdl.handle.net/20.500.12123/4819 1471-9053 https://doi.org/10.1093/pcp/pcy191 eng info:eu-repo/semantics/restrictedAccess application/pdf Oxford University Press Plant and Cell Physiology 59 (11) : 2188-2203 (Noviembre 2018) |