Gel-based proteomic map of Arabidopsis thaliana root plastids and mitochondria.


Journal

BMC plant biology
ISSN: 1471-2229
Titre abrégé: BMC Plant Biol
Pays: England
ID NLM: 100967807

Informations de publication

Date de publication:
04 Sep 2020
Historique:
received: 12 06 2020
accepted: 30 08 2020
entrez: 5 9 2020
pubmed: 6 9 2020
medline: 20 2 2021
Statut: epublish

Résumé

Non-photosynthetic plastids of plants are known to be involved in a range of metabolic and biosynthetic reactions, even if they have been difficult to study due to their small size and lack of color. The morphology of root plastids is heterogeneous and also the plastid size, density and subcellular distribution varies depending on the cell type and developmental stage, and therefore the functional features have remained obscure. Although the root plastid proteome is likely to reveal specific functional features, Arabidopsis thaliana root plastid proteome has not been studied to date. In the present study, we separated Arabidopsis root protein fraction enriched with plastids and mitochondria by 2D-PAGE and identified 84 plastid-targeted and 77 mitochondrion-targeted proteins using LC-MS/MS. The most prevalent root plastid protein categories represented amino acid biosynthesis, carbohydrate metabolism and lipid biosynthesis pathways, while the enzymes involved in starch and sucrose metabolism were not detected. Mitochondrion-targeted proteins were classified mainly into the energetics category. This is the first study presenting gel-based map of Arabidopsis thaliana root plastid and mitochondrial proteome. Our findings suggest that Arabidopsis root plastids have broad biosynthetic capacity, and that they do not play a major role in a long-term storage of carbohydrates. The proteomic map provides a tool for further studies to compare changes in the proteome, e.g. in response to environmental cues, and emphasizes the role of root plastids in nitrogen and sulfur metabolism as well as in amino acid and fatty acid biosynthesis. The results enable taking a first step towards an integrated view of root plastid/mitochondrial proteome and metabolic functions in Arabidopsis thaliana roots.

Sections du résumé

BACKGROUND BACKGROUND
Non-photosynthetic plastids of plants are known to be involved in a range of metabolic and biosynthetic reactions, even if they have been difficult to study due to their small size and lack of color. The morphology of root plastids is heterogeneous and also the plastid size, density and subcellular distribution varies depending on the cell type and developmental stage, and therefore the functional features have remained obscure. Although the root plastid proteome is likely to reveal specific functional features, Arabidopsis thaliana root plastid proteome has not been studied to date.
RESULTS RESULTS
In the present study, we separated Arabidopsis root protein fraction enriched with plastids and mitochondria by 2D-PAGE and identified 84 plastid-targeted and 77 mitochondrion-targeted proteins using LC-MS/MS. The most prevalent root plastid protein categories represented amino acid biosynthesis, carbohydrate metabolism and lipid biosynthesis pathways, while the enzymes involved in starch and sucrose metabolism were not detected. Mitochondrion-targeted proteins were classified mainly into the energetics category.
CONCLUSIONS CONCLUSIONS
This is the first study presenting gel-based map of Arabidopsis thaliana root plastid and mitochondrial proteome. Our findings suggest that Arabidopsis root plastids have broad biosynthetic capacity, and that they do not play a major role in a long-term storage of carbohydrates. The proteomic map provides a tool for further studies to compare changes in the proteome, e.g. in response to environmental cues, and emphasizes the role of root plastids in nitrogen and sulfur metabolism as well as in amino acid and fatty acid biosynthesis. The results enable taking a first step towards an integrated view of root plastid/mitochondrial proteome and metabolic functions in Arabidopsis thaliana roots.

Identifiants

pubmed: 32887556
doi: 10.1186/s12870-020-02635-6
pii: 10.1186/s12870-020-02635-6
pmc: PMC7650296
doi:

Substances chimiques

Plant Proteins 0
Proteome 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

413

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Auteurs

Magda Grabsztunowicz (M)

Molecular Plant Biology, University of Turku, 20520, Turku, Finland.

Anne Rokka (A)

Turku Bioscience Centre, University of Turku and Åbo Akademi University, 20520, Turku, Finland.

Irum Farooq (I)

Molecular Plant Biology, University of Turku, 20520, Turku, Finland.

Eva-Mari Aro (EM)

Molecular Plant Biology, University of Turku, 20520, Turku, Finland.

Paula Mulo (P)

Molecular Plant Biology, University of Turku, 20520, Turku, Finland. pmulo@utu.fi.

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