Regulation of plant ferritin synthesis: how and why

Briat, Jean‐François; Lobréaux, Stéphane; Grignon, Nicole; Vansuyt, Gérard

doi:10.1007/s000180050014

Cited by 125 publications

(97 citation statements)

References 78 publications

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“…Although no experimental demonstration is currently available, this structural observation strongly suggests that all plant ferritin subunits encoded by the four AtFer genes are located within plastids. This is in agreement with electron microscopy studies and immunocytological and biochemical results that demonstrate the presence of this protein in this subcellular compartment in many plant species [10]. The second part of this N-terminal extension is conserved in the four ferritin subunits and shares similarities with previously described extension peptides [28].…”

Section: Discussionsupporting

confidence: 91%

“…The first part of this extension presents all the characteristics of a plastid transit peptide [26]. Furthermore, amino acid sequence analysis of the four AtFer polypeptides, with ChloroP software [27], predicts their targeting to the plastids, in agreement with the localization of the plant ferritin protein reported previously [10,25]. The four mature ferritin subunits possess a plant-specific sequence named extension peptide (EP), which is observed in other plant ferritin subunit sequences reported previously.…”

Section: Amino Acid Sequence Comparison Of the Four A Thaliana Ferrisupporting

confidence: 82%

“…Some members have been characterized and shown to be expressed differentially in response to environmental signals or in the course of development [8,9]. In addition, no IRE sequence is found in the 5h untranslated region (UTR) of plant ferritin mRNA or genes characterized so far [10]. Consistent with such a structural observation is a report of the transcriptional control of a soybean ferritin gene in response to iron excess [6].…”

Section: Introductionmentioning

confidence: 94%

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Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family

PETIT

Briat

Lobréaux

2001

Biochemical Journal

136

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Four ferritin genes are found within the complete sequence of the Arabidopsis thaliana genome. All of them are expressed and their corresponding cDNA species have been cloned. The polypeptide sequences deduced from these four genes confirm all the properties of the ferritin subunits described so far, non-exhaustively, from various plant species. All are predicted to be targeted to the plastids, which is consistent with the existence of a putative transit peptide at their N-terminal extremity. They also all possess a conserved extension peptide in the mature subunit. Specific residues for ferroxidase activity and iron nucleation, which are found respectively in H-type or L-type ferritin subunits in animals, are both conserved within each of the four A. thaliana ferritin polypeptides. In addition, the hydrophilic nature of the plant ferritin E-helix is conserved in the four A. thaliana ferritin subunits. Besides this strong structural conservation, the four genes are differentially expressed in response to various environmental signals, and during the course of plant growth and development. AtFer1 and AtFer3 are the two major genes expressed in response to treatment with an iron overload. Under our experimental conditions, AtFer4 is expressed with different kinetics and AtFer2 is not responsive to iron. H2O2 activates the expression of AtFer1 and, to a smaller extent, AtFer3. Abscisic acid promotes the expression of only AtFer2, which is consistent with the observation that this is the only gene of the four to be expressed in seeds, whereas AtFer1, AtFer4 and AtFer3 are expressed in various vegetative organs but not in seeds.

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Section: Discussionsupporting

confidence: 91%

Section: Amino Acid Sequence Comparison Of the Four A Thaliana Ferrisupporting

confidence: 82%

Section: Introductionmentioning

confidence: 94%

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Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family

PETIT

Briat

Lobréaux

2001

Biochemical Journal

136

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“…120). The preferential accumulation of Ferritin 1 (TC293195) in the M membrane is consistent with these observations and supports a role in iron chelation to reduce formation of reactive hydroxyl radicals by interaction of O 2 with ferrous ions as suggested previously (120).…”

Section: Purification Of M and Bs Chloroplast Membranes Fromsupporting

confidence: 90%

Consequences of C4 Differentiation for Chloroplast Membrane Proteomes in Maize Mesophyll and Bundle Sheath Cells

Majeran

Zybailov

Ytterberg

et al. 2008

Molecular & Cellular Proteomics

192

205

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Chloroplasts of maize leaves differentiate into specific bundle sheath (BS) and mesophyll (M) types to accommodate C 4 photosynthesis. Chloroplasts contain thylakoid and envelope membranes that contain the photosynthetic machineries and transporters but also proteins involved in e.g. protein homeostasis. These chloroplast membranes must be specialized within each cell type to accommodate C 4 photosynthesis and regulate metabolic fluxes and activities. This quantitative study determined the differentiated state of BS and M chloroplast thylakoid and envelope membrane proteomes and their oligomeric states using innovative gel-based and mass spectrometry-based protein quantifications. This included native gels, iTRAQ, and label-free quantification using an LTQ-Orbitrap. Subunits of Photosystems I and II, the cytochrome b 6 f, and ATP synthase complexes showed average BS/M accumulation ratios of 1.6, 0.45, 1.0, and 1.33, respectively, whereas ratios for the light-harvesting complex I and II families were 1.72 and 0.68, respectively. A 1000-kDa BS-specific NAD(P)H dehydrogenase complex with associated proteins of unknown function containing more than 15 proteins was observed; we speculate that this novel complex possibly functions in inorganic carbon concentration when carboxylation rates by ribulose-bisphosphate carboxylase/oxygenase are lower than decarboxylation rates by malic enzyme. In leaves of C 4 grasses such as maize (Zea mays), photosynthetic activities are partitioned between two morphologically and biochemically distinct bundle sheath (BS) 1 and mesophyll (M) cells. A single ring of BS cells surrounds the vascular bundle followed by a concentric ring of specialized M cells, creating the classical Kranz anatomy. C 4 differentiation occurs along a developmental gradient with proplastids at the leaf base and fully differentiated C 4 M and BS chloroplasts at the leaf tip. Genetic screens for mutants affected in BS differentiation identified various mutants (1-4). However, the molecular basis for C 4 differentiation is still poorly understood but includes transcriptional regulation through DNA regulatory elements, transcription factors, and likely also metabolic signals (5, 6). Differential accumulation of thylakoid proteases (Egy andDegP

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“…Fe is essential as central ion in heme proteins (e.g., in cytochromes, nitrate reductase, catalase, and peroxidase), in siroheme proteins (e.g., nitrite reductase and sulfite reductase), in iron-sulfur proteins (e.g., ferredoxin) and in other iron-containing proteins (e.g., lipoxygenases) [1,2,[13][14][15][16]. Ferritin is located in plastids and represents important intracellular storage form for Fe [17][18][19]. Mn is essential for the oxygen evolution in photosystem II and for a series of enzymatic reactions (e.g., phosphoenolpyruvate carboxykinase, and superoxide dismutase) [1,2,13,[20][21][22].…”

Section: Heavy Metals: Micronutrients or Pollutants?mentioning

confidence: 99%

Heavy Metals in Crop Plants: Transport and Redistribution Processes on the Whole Plant Level

2015

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Abstract:Copper, zinc, manganese, iron, nickel and molybdenum are essential micronutrients for plants. However, when present in excess they may damage the plant or decrease the quality of harvested plant products. Some other heavy metals such as cadmium, lead or mercury are not needed by plants and represent pollutants. The uptake into the roots, the loading into the xylem, the acropetal transport to the shoot with the transpiration stream and the further redistribution in the phloem are crucial for the distribution in aerial plant parts. This review is focused on long-distance transport of heavy metals via xylem and phloem and on interactions between the two transport systems. Phloem transport is the basis for the redistribution within the shoot and for the accumulation in fruits and seeds. Solutes may be transferred from the xylem to the phloem (e.g., in the small bundles in stems of cereals, in minor leaf veins). Nickel is highly phloem-mobile and directed to expanding plant parts. Zinc and to a lesser degree also cadmium are also mobile in the phloem and accumulate in meristems (root tips, shoot apex, axillary buds). Iron and manganese are characterized by poor phloem mobility and are retained in older leaves.

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Regulation of plant ferritin synthesis: how and why

Cited by 125 publications

References 78 publications

Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family

Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family

Consequences of C4 Differentiation for Chloroplast Membrane Proteomes in Maize Mesophyll and Bundle Sheath Cells

Heavy Metals in Crop Plants: Transport and Redistribution Processes on the Whole Plant Level

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