Overexpression of glycine-rich RNA-binding protein in tomato renders fruits with higher protein content after cold storage

Glycine-rich RNA-binding proteins (GR-RBPs) are involved in RNA processing and also some of them are output signals of the circadian clock. In tomato, one GR-RBP gene family (LeGRP1) is composed by three highly homologous genes (LeGRP1a-c); each one rendering three transcriptional products: the un-s...

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Autores principales: Ruggieri, Germán, Triassi, Agustina, Alvarez, Clarisa E., Gola, Aldana, Wiggenhauser, Julieta, Budde, Claudio Olaf, Lara, María Valeria, Müller, Gabriela Leticia
Formato: Artículo
Lenguaje:Inglés
Publicado: 2018
Materias:
Acceso en línea:https://link.springer.com/article/10.1007%2Fs10535-018-0794-3
http://hdl.handle.net/20.500.12123/2422
https://doi.org/10.1007/s10535-018-0794-3
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author Ruggieri, Germán
Triassi, Agustina
Alvarez, Clarisa E.
Gola, Aldana
Wiggenhauser, Julieta
Budde, Claudio Olaf
Lara, María Valeria
Müller, Gabriela Leticia
author_browse Alvarez, Clarisa E.
Budde, Claudio Olaf
Gola, Aldana
Lara, María Valeria
Müller, Gabriela Leticia
Ruggieri, Germán
Triassi, Agustina
Wiggenhauser, Julieta
author_facet Ruggieri, Germán
Triassi, Agustina
Alvarez, Clarisa E.
Gola, Aldana
Wiggenhauser, Julieta
Budde, Claudio Olaf
Lara, María Valeria
Müller, Gabriela Leticia
author_sort Ruggieri, Germán
collection INTA Digital
description Glycine-rich RNA-binding proteins (GR-RBPs) are involved in RNA processing and also some of them are output signals of the circadian clock. In tomato, one GR-RBP gene family (LeGRP1) is composed by three highly homologous genes (LeGRP1a-c); each one rendering three transcriptional products: the un-spliced pre-RNA (preLegrp1a-c), the mature mRNA (mLegrp1a-c) and the alternatively spliced mRNA (asLegrp1a-c). To get insight into their regulation and impact on RNA metabolism in fruits, Solanum lycopersicum cv. Micro-Tom was transformed with preLeGRP1a fused to the polygalacturonase promoter, which drives expression to fruits from the mature green stage. Our results demonstrated a complex positive regulation of LeGRPs, in which LeGRP1a overexpression led to the induction of the others LeGRP1 members. Even though the LeGRP1 transcription and the content of three LeGRPs proteins were affected, the overall LeGRP protein circadian rhythm profile was similar in transgenic and WT fruits. However, when the fruits are kept at chilling temperature after harvest, total protein content was significantly higher in transgenic than in WT fruits, and the content of some free amino acids was modified. The results obtained suggest a probable role of LeGRP1s: structural rearrangements and/or stabilization of mRNA to allow efficient processing of fruits under cold conditions.
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spelling INTA24222018-08-21T15:51:04Z Overexpression of glycine-rich RNA-binding protein in tomato renders fruits with higher protein content after cold storage Ruggieri, Germán Triassi, Agustina Alvarez, Clarisa E. Gola, Aldana Wiggenhauser, Julieta Budde, Claudio Olaf Lara, María Valeria Müller, Gabriela Leticia Tomate Solanum lycopersicum Aminoácidos Ritmo Circadiano Poligalacturonasa ARN Almacenamiento en frío Proteínas Tomatoes Amino Acids Circadian Rhythm Polygalacturonase RNA Cold Storage Proteins Lycopersicon esculentum Glycine-rich RNA-binding proteins (GR-RBPs) are involved in RNA processing and also some of them are output signals of the circadian clock. In tomato, one GR-RBP gene family (LeGRP1) is composed by three highly homologous genes (LeGRP1a-c); each one rendering three transcriptional products: the un-spliced pre-RNA (preLegrp1a-c), the mature mRNA (mLegrp1a-c) and the alternatively spliced mRNA (asLegrp1a-c). To get insight into their regulation and impact on RNA metabolism in fruits, Solanum lycopersicum cv. Micro-Tom was transformed with preLeGRP1a fused to the polygalacturonase promoter, which drives expression to fruits from the mature green stage. Our results demonstrated a complex positive regulation of LeGRPs, in which LeGRP1a overexpression led to the induction of the others LeGRP1 members. Even though the LeGRP1 transcription and the content of three LeGRPs proteins were affected, the overall LeGRP protein circadian rhythm profile was similar in transgenic and WT fruits. However, when the fruits are kept at chilling temperature after harvest, total protein content was significantly higher in transgenic than in WT fruits, and the content of some free amino acids was modified. The results obtained suggest a probable role of LeGRP1s: structural rearrangements and/or stabilization of mRNA to allow efficient processing of fruits under cold conditions. EEA San Pedro Fil: Ruggieri, German. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Triassi, Agustina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Álvarez, Clarisa. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Gola, Aldana. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Wiggenhauser, Julieta. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Budde, Claudio Olaf. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria San Pedro; Argentina Fil: Lara, Maria Valeria. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Drincovich, Maria F. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina Fil: Müller, Gabriela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Centro de Estudios Fotosintéticos y Bioquímicos; Argentina 2018-05-17T17:34:15Z 2018-05-17T17:34:15Z 2018 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/acceptedVersion https://link.springer.com/article/10.1007%2Fs10535-018-0794-3 http://hdl.handle.net/20.500.12123/2422 1573-8264 0006-3134 https://doi.org/10.1007/s10535-018-0794-3 eng info:eu-repo/semantics/embargoedAccess application/pdf Biologia Plantarum 62 (3) : 501-510 (2018)
spellingShingle Tomate
Solanum lycopersicum
Aminoácidos
Ritmo Circadiano
Poligalacturonasa
ARN
Almacenamiento en frío
Proteínas
Tomatoes
Amino Acids
Circadian Rhythm
Polygalacturonase
RNA
Cold Storage
Proteins
Lycopersicon esculentum
Ruggieri, Germán
Triassi, Agustina
Alvarez, Clarisa E.
Gola, Aldana
Wiggenhauser, Julieta
Budde, Claudio Olaf
Lara, María Valeria
Müller, Gabriela Leticia
Overexpression of glycine-rich RNA-binding protein in tomato renders fruits with higher protein content after cold storage
title Overexpression of glycine-rich RNA-binding protein in tomato renders fruits with higher protein content after cold storage
title_full Overexpression of glycine-rich RNA-binding protein in tomato renders fruits with higher protein content after cold storage
title_fullStr Overexpression of glycine-rich RNA-binding protein in tomato renders fruits with higher protein content after cold storage
title_full_unstemmed Overexpression of glycine-rich RNA-binding protein in tomato renders fruits with higher protein content after cold storage
title_short Overexpression of glycine-rich RNA-binding protein in tomato renders fruits with higher protein content after cold storage
title_sort overexpression of glycine rich rna binding protein in tomato renders fruits with higher protein content after cold storage
topic Tomate
Solanum lycopersicum
Aminoácidos
Ritmo Circadiano
Poligalacturonasa
ARN
Almacenamiento en frío
Proteínas
Tomatoes
Amino Acids
Circadian Rhythm
Polygalacturonase
RNA
Cold Storage
Proteins
Lycopersicon esculentum
url https://link.springer.com/article/10.1007%2Fs10535-018-0794-3
http://hdl.handle.net/20.500.12123/2422
https://doi.org/10.1007/s10535-018-0794-3
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