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-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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Main Authors: Ruggieri, Germán, Triassi, Agustina, Alvarez, Clarisa E., Gola, Aldana, Wiggenhauser, Julieta, Budde, Claudio Olaf, Lara, María Valeria, Müller, Gabriela Leticia
Format: info:ar-repo/semantics/artículo biblioteca
Language:eng
Published: 2018
Subjects:Tomate, Solanum lycopersicum, Aminoácidos, Ritmo Circadiano, Poligalacturonasa, ARN, Almacenamiento en frío, Proteínas, Tomatoes, Amino Acids, Circadian Rhythm, Polygalacturonase, RNA, Cold Storage, Proteins, Lycopersicon esculentum,
Online Access: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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spelling oai:localhost:20.500.12123-24222018-08-21T15:51:04Z 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)
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 Tomate
Solanum lycopersicum
Aminoácidos
Ritmo Circadiano
Poligalacturonasa
ARN
Almacenamiento en frío
Proteínas
Tomatoes
Amino Acids
Circadian Rhythm
Polygalacturonase
RNA
Cold Storage
Proteins
Lycopersicon esculentum
Tomate
Solanum lycopersicum
Aminoácidos
Ritmo Circadiano
Poligalacturonasa
ARN
Almacenamiento en frío
Proteínas
Tomatoes
Amino Acids
Circadian Rhythm
Polygalacturonase
RNA
Cold Storage
Proteins
Lycopersicon esculentum
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
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
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.
format info:ar-repo/semantics/artículo
topic_facet Tomate
Solanum lycopersicum
Aminoácidos
Ritmo Circadiano
Poligalacturonasa
ARN
Almacenamiento en frío
Proteínas
Tomatoes
Amino Acids
Circadian Rhythm
Polygalacturonase
RNA
Cold Storage
Proteins
Lycopersicon esculentum
author Ruggieri, Germán
Triassi, Agustina
Alvarez, Clarisa E.
Gola, Aldana
Wiggenhauser, Julieta
Budde, Claudio Olaf
Lara, María Valeria
Müller, Gabriela Leticia
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
title 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_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_sort overexpression of glycine-rich rna-binding protein in tomato renders fruits with higher protein content after cold storage
publishDate 2018
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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