Aconitase: To Be or not to Be Inside Plant Glyoxysomes, That Is the Question

Bellis, Luigi De; Luvisi, Andrea; Alpi, Amedeo

doi:10.3390/biology9070162

Cited by 12 publications

(8 citation statements)

References 68 publications

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“…Overall, our BiFC data agree with the previously reported localization of B'ζ to both the mitochondrion and the cytoplasm [7]. ACO3 is an iron-sulfur-containing hydratase that is dually targeted to the mitochondrion and the cytoplasm in plants and yeast [26,32,33]. Mitochondrial ACO3 is active in the Krebs cycle, where it catalyzes the stereo-specific isomerization of citrate to isocitrate.…”

Section: Verification Of B'ζ Putative Interactors Involved In Energy ...supporting

confidence: 91%

“…Since all of the candidates except mSFC are part of multigene families in Arabidopsis, we carefully chose for each protein the paralog that was most relevant for our study. For example, ACO3 carries out the main aconitase activity of the three Arabidopsis ACOs [26], and FUM1 was preferred over FUM2 since it is mitochondrion-targeted and is essential (i.e., FUM2 cannot compensate for a lack of FUM1) [27].…”

Section: Sugar Dependence Assay Points To a Role In Energy Metabolismmentioning

confidence: 99%

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Protein–Protein Interactions and Quantitative Phosphoproteomic Analysis Reveal Potential Mitochondrial Substrates of Protein Phosphatase 2A-B’ζ Holoenzyme

Elshobaky

Lillo

Hodén

et al. 2023

Plants

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Protein phosphatase 2A (PP2A) is a heterotrimeric conserved serine/threonine phosphatase complex that includes catalytic, scaffolding, and regulatory subunits. The 3 A subunits, 17 B subunits, and 5 C subunits that are encoded by the Arabidopsis genome allow 255 possible PP2A holoenzyme combinations. The regulatory subunits are crucial for substrate specificity and PP2A complex localization and are classified into the B, B’, and B” non-related families in land plants. In Arabidopsis, the close homologs B’η, B’θ, B’γ, and B’ζ are further classified into a subfamily of B’ called B’η. Previous studies have suggested that mitochondrial targeted PP2A subunits (B’ζ) play a role in energy metabolism and plant innate immunity. Potentially, the PP2A-B’ζ holoenzyme is involved in the regulation of the mitochondrial succinate/fumarate translocator, and it may affect the enzymes involved in energy metabolism. To investigate this hypothesis, the interactions between PP2A-B’ζ and the enzymes involved in the mitochondrial energy flow were investigated using bimolecular fluorescence complementation in tobacco and onion cells. Interactions were confirmed between the B’ζ subunit and the Krebs cycle proteins succinate/fumarate translocator (mSFC1), malate dehydrogenase (mMDH2), and aconitase (ACO3). Additional putative interacting candidates were deduced by comparing the enriched phosphoproteomes of wild type and B’ζ mutants: the mitochondrial regulator Arabidopsis pentatricopeptide repeat 6 (PPR6) and the two metabolic enzymes phosphoenolpyruvate carboxylase (PPC3) and phosphoenolpyruvate carboxykinase (PCK1). Overall, this study identifies potential PP2A substrates and highlights the role of PP2A in regulating energy metabolism in mitochondria.

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Section: Verification Of B'ζ Putative Interactors Involved In Energy ...supporting

confidence: 91%

Section: Sugar Dependence Assay Points To a Role In Energy Metabolismmentioning

confidence: 99%

Protein–Protein Interactions and Quantitative Phosphoproteomic Analysis Reveal Potential Mitochondrial Substrates of Protein Phosphatase 2A-B’ζ Holoenzyme

Elshobaky

Lillo

Hodén

et al. 2023

Plants

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“…Mitochondrial aconitase is an enzyme within the TCA cycle that facilitates the conversion of citrate to isocitrate. 84 We investigated seed mitochondrial aconitase activity using the Aconitase Assay Kit (MAK337, Sigma-Aldrich, USA) according to the manufacturer’s instructions. Briefly, 100 mg of each 0 and 15-day seeds were extracted.…”

Section: Methodsmentioning

confidence: 99%

Comparative Proteomic Analysis of Ridge Gourd Seed (Luffa acutangula (L.) Roxb.) during Artificial Aging

Kumsab,

Yingchutrakul,

Simanon

et al. 2024

ACS Omega

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Seed aging is a complicated process influenced by environmental conditions, impacting biochemical processes in seeds and causing deterioration that results in reduced viability and vigor. In this study, we investigated the seed aging process of ridge gourd, which is one of the most exported commercial seeds in Thailand using sequential window acquisition of all theoretical fragment ion spectra mass spectrometry. A total of 855 proteins were identified among the two groups (0 d/15 d and 0 d/30 d). The Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analyses of differentially expressed proteins revealed that in ridge gourd seeds, the aging process altered the abundance of proteins related to the oxidative stress response, nutrient reservoir, and metabolism pathway. The most identified DEPs were mitochondrial proteins, ubiquitin−proteasome system proteins, ribosomal proteins, carbohydrate metabolism-related proteins, and stress response-related proteins. This study also presented the involvement of aconitase and glutathione pathway-associated enzymes in seed aging, with aconitase and total glutathione being determined as possible suggestive biomarkers for aged ridge gourd seeds. This acquired knowledge has the potential to considerably improve growing methods and seed preservation techniques, enhancing seed storage and maintenance.

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“…Three additional enzymes also participate in the TCA cycle: citrate synthase, aconitase, and malate dehydrogenase. This cycle is distributed between different cell compartments and likely involves a very close coordination between glyoxysomes and mitochondria [ 132 ]. Four-carbon compounds from the glyoxylate cycle can be converted into hexoses by gluconeogenesis and subsequently converted into sucrose.…”

Section: Biological Functions Of Oils Stored In the Endospermmentioning

confidence: 99%

Molecular Control of Oil Metabolism in the Endosperm of Seeds

Miray

Kazaz

et al. 2021

IJMS

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In angiosperm seeds, the endosperm develops to varying degrees and accumulates different types of storage compounds remobilized by the seedling during early post-germinative growth. Whereas the molecular mechanisms controlling the metabolism of starch and seed-storage proteins in the endosperm of cereal grains are relatively well characterized, the regulation of oil metabolism in the endosperm of developing and germinating oilseeds has received particular attention only more recently, thanks to the emergence and continuous improvement of analytical techniques allowing the evaluation, within a spatial context, of gene activity on one side, and lipid metabolism on the other side. These studies represent a fundamental step toward the elucidation of the molecular mechanisms governing oil metabolism in this particular tissue. In particular, they highlight the importance of endosperm-specific transcriptional controls for determining original oil compositions usually observed in this tissue. In the light of this research, the biological functions of oils stored in the endosperm of seeds then appear to be more diverse than simply constituting a source of carbon made available for the germinating seedling.

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Aconitase: To Be or not to Be Inside Plant Glyoxysomes, That Is the Question

Cited by 12 publications

References 68 publications

Protein–Protein Interactions and Quantitative Phosphoproteomic Analysis Reveal Potential Mitochondrial Substrates of Protein Phosphatase 2A-B’ζ Holoenzyme

Protein–Protein Interactions and Quantitative Phosphoproteomic Analysis Reveal Potential Mitochondrial Substrates of Protein Phosphatase 2A-B’ζ Holoenzyme

Comparative Proteomic Analysis of Ridge Gourd Seed (Luffa acutangula (L.) Roxb.) during Artificial Aging

Molecular Control of Oil Metabolism in the Endosperm of Seeds

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