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.

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Main Authors: 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
Format: info:ar-repo/semantics/artículo biblioteca
Language:eng
Published: Oxford University Press 2018-11
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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record_format koha
institution INTA AR
collection DSpace
country Argentina
countrycode AR
component Bibliográfico
access En linea
databasecode dig-inta-ar
tag biblioteca
region America del Sur
libraryname Biblioteca Central del INTA Argentina
language eng
topic Tomatoes
Tocopherols
Chloroplasts
Proteins
Tomate
Tocoferoles
Cloroplasto
Proteínas
Tomatoes
Tocopherols
Chloroplasts
Proteins
Tomate
Tocoferoles
Cloroplasto
Proteínas
spellingShingle 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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spelling 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)