Changes in the microsomal proteome of tomato fruit during ripening

The variations in the membrane proteome of tomato fruit pericarp during ripening have been investigated by mass spectrometry-based label-free proteomics. Mature green (MG30) and red ripe (R45) stages were chosen because they are pivotal in the ripening process: MG30 corresponds to the end of cellula...

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Published inScientific reports Vol. 9; no. 1; pp. 14350 - 18
Main Authors Pontiggia, Daniela, Spinelli, Francesco, Fabbri, Claudia, Licursi, Valerio, Negri, Rodolfo, De Lorenzo, Giulia, Mattei, Benedetta
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 04.10.2019
Nature Publishing Group
Subjects
631/449/2653
631/449/2679/2684
82
82/16
82/29
82/58
Biosynthesis
Cell walls
Fractionation
Fruit - chemistry
Fruit - cytology
Fruit - growth & development
Fruit - metabolism
Fruits
Gene Expression Regulation, Developmental
Gene Expression Regulation, Plant
Humanities and Social Sciences
Lipid metabolism
Lycopersicon esculentum - chemistry
Lycopersicon esculentum - cytology
Lycopersicon esculentum - growth & development
Lycopersicon esculentum - metabolism
Mass Spectrometry
Mass spectroscopy
Menopause
Metabolism
Microsomes - chemistry
Microsomes - metabolism
multidisciplinary
Peptides
Pericarp
Protein biosynthesis
Protein synthesis
Protein turnover
Proteins
Proteome - analysis
Proteome - metabolism
Proteomics
Proteomics - methods
Ripening
Science
Science (multidisciplinary)
Tomatoes
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Abstract The variations in the membrane proteome of tomato fruit pericarp during ripening have been investigated by mass spectrometry-based label-free proteomics. Mature green (MG30) and red ripe (R45) stages were chosen because they are pivotal in the ripening process: MG30 corresponds to the end of cellular expansion, when fruit growth has stopped and fruit starts ripening, whereas R45 corresponds to the mature fruit. Protein patterns were markedly different: among the 1315 proteins identified with at least two unique peptides, 145 significantly varied in abundance in the process of fruit ripening. The subcellular and biochemical fractionation resulted in GO term enrichment for organelle proteins in our dataset, and allowed the detection of low-abundance proteins that were not detected in previous proteomic studies on tomato fruits. Functional annotation showed that the largest proportion of identified proteins were involved in cell wall metabolism, vesicle-mediated transport, hormone biosynthesis, secondary metabolism, lipid metabolism, protein synthesis and degradation, carbohydrate metabolic processes, signalling and response to stress.
AbstractList The variations in the membrane proteome of tomato fruit pericarp during ripening have been investigated by mass spectrometry-based label-free proteomics. Mature green (MG30) and red ripe (R45) stages were chosen because they are pivotal in the ripening process: MG30 corresponds to the end of cellular expansion, when fruit growth has stopped and fruit starts ripening, whereas R45 corresponds to the mature fruit. Protein patterns were markedly different: among the 1315 proteins identified with at least two unique peptides, 145 significantly varied in abundance in the process of fruit ripening. The subcellular and biochemical fractionation resulted in GO term enrichment for organelle proteins in our dataset, and allowed the detection of low-abundance proteins that were not detected in previous proteomic studies on tomato fruits. Functional annotation showed that the largest proportion of identified proteins were involved in cell wall metabolism, vesicle-mediated transport, hormone biosynthesis, secondary metabolism, lipid metabolism, protein synthesis and degradation, carbohydrate metabolic processes, signalling and response to stress.
The variations in the membrane proteome of tomato fruit pericarp during ripening have been investigated by mass spectrometry-based label-free proteomics. Mature green (MG30) and red ripe (R45) stages were chosen because they are pivotal in the ripening process: MG30 corresponds to the end of cellular expansion, when fruit growth has stopped and fruit starts ripening, whereas R45 corresponds to the mature fruit. Protein patterns were markedly different: among the 1315 proteins identified with at least two unique peptides, 145 significantly varied in abundance in the process of fruit ripening. The subcellular and biochemical fractionation resulted in GO term enrichment for organelle proteins in our dataset, and allowed the detection of low-abundance proteins that were not detected in previous proteomic studies on tomato fruits. Functional annotation showed that the largest proportion of identified proteins were involved in cell wall metabolism, vesicle-mediated transport, hormone biosynthesis, secondary metabolism, lipid metabolism, protein synthesis and degradation, carbohydrate metabolic processes, signalling and response to stress.The variations in the membrane proteome of tomato fruit pericarp during ripening have been investigated by mass spectrometry-based label-free proteomics. Mature green (MG30) and red ripe (R45) stages were chosen because they are pivotal in the ripening process: MG30 corresponds to the end of cellular expansion, when fruit growth has stopped and fruit starts ripening, whereas R45 corresponds to the mature fruit. Protein patterns were markedly different: among the 1315 proteins identified with at least two unique peptides, 145 significantly varied in abundance in the process of fruit ripening. The subcellular and biochemical fractionation resulted in GO term enrichment for organelle proteins in our dataset, and allowed the detection of low-abundance proteins that were not detected in previous proteomic studies on tomato fruits. Functional annotation showed that the largest proportion of identified proteins were involved in cell wall metabolism, vesicle-mediated transport, hormone biosynthesis, secondary metabolism, lipid metabolism, protein synthesis and degradation, carbohydrate metabolic processes, signalling and response to stress.
ArticleNumber 14350
Author Pontiggia, Daniela
Fabbri, Claudia
Licursi, Valerio
Spinelli, Francesco
De Lorenzo, Giulia
Mattei, Benedetta
Negri, Rodolfo
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  fullname: De Lorenzo, Giulia
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  organization: Department of Life, Health and Environmental Sciences, University of L’Aquila
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SSID ssj0000529419
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Snippet The variations in the membrane proteome of tomato fruit pericarp during ripening have been investigated by mass spectrometry-based label-free proteomics....
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proquest
pubmed
crossref
springer
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Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 14350
SubjectTerms 631/449/2653
631/449/2679/2684
82
82/16
82/29
82/58
Biosynthesis
Cell walls
Fractionation
Fruit - chemistry
Fruit - cytology
Fruit - growth & development
Fruit - metabolism
Fruits
Gene Expression Regulation, Developmental
Gene Expression Regulation, Plant
Humanities and Social Sciences
Lipid metabolism
Lycopersicon esculentum - chemistry
Lycopersicon esculentum - cytology
Lycopersicon esculentum - growth & development
Lycopersicon esculentum - metabolism
Mass Spectrometry
Mass spectroscopy
Menopause
Metabolism
Microsomes - chemistry
Microsomes - metabolism
multidisciplinary
Peptides
Pericarp
Protein biosynthesis
Protein synthesis
Protein turnover
Proteins
Proteome - analysis
Proteome - metabolism
Proteomics
Proteomics - methods
Ripening
Science
Science (multidisciplinary)
Tomatoes
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Title Changes in the microsomal proteome of tomato fruit during ripening
URI https://link.springer.com/article/10.1038/s41598-019-50575-5
https://www.ncbi.nlm.nih.gov/pubmed/31586085
https://www.proquest.com/docview/2300956039
https://www.proquest.com/docview/2301443255
https://pubmed.ncbi.nlm.nih.gov/PMC6778153
Volume 9
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