The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi

Giorgi, Alessandra; Mignogna, Giuseppina; Bellapadrona, Giuliano; Gattoni, Maurizio; Chiaraluce, Roberta; Consalvi, Valerio; Chiancone, Emilia; Stefanini, Simonetta

doi:10.1016/j.abb.2008.06.022

Cited by 50 publications

(45 citation statements)

References 26 publications

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“…This view is supported by previous studies indicating that the L-chain facilitates mineral formation in horse spleen ferritin, presumably because of increased iron turnover at the ferroxidase site of the H-chain in the presence of the L-chain (42). In contrast, such cooperative interaction seems to be lacking in the H/M heteropolymer found in fish as indicated by the fact that the co-assembly of Hand M-chains in Trematomus newnesi and Trematomus bernacchii liver ferritin results in a decreased catalytic and mineralization efficiency relative to the M homopolymer, which favors adaptation to low temperatures (36,43). These comparative results imply that the specific EP domains of phytoferritin might be responsible, at least partly, for the above observed synergistic interaction between the H-1 and H-2 subunits during oxidative deposition of iron in protein.…”

Section: Discussionmentioning

confidence: 82%

Section: Discussionmentioning

confidence: 94%

“…This property is reminiscent of heteropolymeric H/M(HЈ) ferritins found in the liver of Antarctic teleosts (36). The M subunit displays the features of both H and L subunits (7,36), indicating that it is an H and L hybrid subunit. Similarly, all subunits in phytoferritin characterized thus far likewise contain both a typical H-type ferroxidase center and all of the amino acid residues characteristic of an L-type subunit for efficient iron nucleation with the cavity (11).…”

Section: Discussionmentioning

confidence: 94%

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Role of H-1 and H-2 Subunits of Soybean Seed Ferritin in Oxidative Deposition of Iron in Protein

Deng

Liao

Yang

et al. 2010

Journal of Biological Chemistry

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Naturally occurring phytoferritin is a heteropolymer consisting of two different H-type subunits, H-1 and H-2. Prior to this study, however, the function of the two subunits in oxidative deposition of iron in ferritin was unknown. The data show that, upon aerobic addition of 48 -200 Fe 2؉ /shell to apoferritin, iron oxidation occurs only at the diiron ferroxidase center of recombinant H1 (rH-1). In addition to the diiron ferroxidase mechanism, such oxidation is catalyzed by the extension peptide (a specific domain found in phytoferritin) of rH-2, because the H-1 subunit is able to remove Fe 3؉ from the center to the inner cavity better than the H-2 subunit. These findings support the idea that the H-1 and H-2 subunits play different roles in iron mineralization in protein. Interestingly, at medium iron loading (200 irons/shell), wild-type (WT) soybean seed ferritin (SSF) exhibits a stronger activity in catalyzing iron oxidation (1.10 ؎ 0.13 M iron/subunit/s) than rH-1 (0.59 ؎ 0.07 M iron/subunit/s) and rH-2 (0.48 ؎ 0.04 M iron/subunit/s), demonstrating that a synergistic interaction exists between the H-1 and H-2 subunits in SSF during iron mineralization. Such synergistic interaction becomes considerably stronger at high iron loading (400 irons/shell) as indicated by the observation that the iron oxidation activity of WT SSF is ϳ10 times larger than those of rH-1 and rH-2. This helps elucidate the widespread occurrence of heteropolymeric ferritins in plants.Iron and oxygen chemistry, in a variety of non-heme diiron proteins, has drawn considerable attention because of their various roles in reversible O 2 binding for respiration in hemerythrin, oxidation and desaturation of organic substrates in methane monooxygenase, R2 subunit of ribonucleotide reductase, stearoyl-acyl carrier protein ⌬-9 desaturase, as well as the detoxification and concentration of iron in Dps and ferritin (1-6). Diiron centers have similar structural motifs containing a combination of carboxylate and histidine ligands that either bind or bridge the two metal ions of the dinuclear active site. Although the dinuclear centers of the protein are very similar in structure, each of the proteins fulfills a different biological function that appears to be mediated by the nature of the first and second coordination sphere of the diiron center.Ferritins are a special class of diiron proteins that play a role in both iron housekeeping and iron detoxification. They are widely distributed in animals, plants, and bacteria (but not in yeast) and are typically composed of 24 similar or identical subunits assembled into a shell-like structure. In vertebrates, ferritins consist of two types of subunits, H and L, respectively. The two types have about 55% identity in amino acid sequence.

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Section: Discussionmentioning

confidence: 82%

Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 94%

See 1 more Smart Citation

Role of H-1 and H-2 Subunits of Soybean Seed Ferritin in Oxidative Deposition of Iron in Protein

Deng

Liao

Yang

et al. 2010

Journal of Biological Chemistry

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“…By contrast to their mammal counterparts, ferritins from other vertebrates contain a third subunit type, the middle (M)-chain, which harbors the residues that form both the ferroxidase center and the ferric core nucleation site(s) (Giorgi et al 2008). M or H/M ferritin assemblages are present in lower vertebrates, notably in fish and amphibians (Andersen et al 1995(Andersen et al , 1998Dickey et al 1987).…”

Section: Introductionmentioning

confidence: 99%

“…M or H/M ferritin assemblages are present in lower vertebrates, notably in fish and amphibians (Andersen et al 1995(Andersen et al , 1998Dickey et al 1987). All three chain types are found in amphibians, but only L-chains and H-chains have been found in mammalian FTNs, thereby indicating the existence of a highly specialized L-chain that originated from the tetrapod lineage (Giorgi et al 2008).…”

Section: Introductionmentioning

confidence: 99%

Genome-wide comparison of ferritin family from Archaea, Bacteria, Eukarya, and Viruses: its distribution, characteristic motif, and phylogenetic relationship

Bai

Xie

et al. 2015

Sci Nat

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Ferritins are highly conserved proteins that are widely distributed in various species from archaea to humans. The ubiquitous characteristic of these proteins reflects the pivotal contribution of ferritins to the safe storage and timely delivery of iron to achieve iron homeostasis. This study investigated the ferritin genes in 248 genomes from various species, including viruses, archaea, bacteria, and eukarya. The distribution comparison suggests that mammals and eudicots possess abundant ferritin genes, whereas fungi contain very few ferritin genes. Archaea and bacteria show considerable numbers of ferritin genes. Generally, prokaryotes possess three types of ferritin (the typical ferritin, bacterioferritin, and DNA-binding protein from starved cell), whereas eukaryotes have various subunit types of ferritin, thereby indicating the individuation of the ferritin family during evolution. The characteristic motif analysis of ferritins suggested that all key residues specifying the unique structural motifs of ferritin are highly conserved across three domains of life. Meanwhile, the characteristic motifs were also distinguishable between ferritin groups, especially phytoferritins, which show a plant-specific motif. The phylogenetic analyses show that ferritins within the same subfamily or subunits are generally clustered together. The phylogenetic relationships among ferritin members suggest that both gene duplication and horizontal transfer contribute to the wide variety of ferritins, and their possible evolutionary scenario was also proposed. The results contribute to a better understanding of the distribution, characteristic motif, and evolutionary relationship of the ferritin family.

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Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta

Ming

Huan

et al. 2021

FEBS Open Bio

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For marine invertebrates with no adaptive immune system, ferritin is a major intracellular iron‐storage protein with a critical role in innate immunity. Here, we present the crystal structures of two novel ferritins [Fer147 and Phascolosoma esculenta ferritin (PeFer)] from the marine invertebrate P. esculenta, which resides in muddy‐bottom coastal regions. Fer147 and PeFer exhibit the 4‐3‐2 symmetry of cage‐like hollow shells containing 24 subunits, similar to other known ferritins. Fer147 and PeFer contain both the conserved ferroxidase center and threefold channels. Subtle structural differences in the putative nucleation sites suggest possible routes of metal ion movement in the protein shells. However, the marked variation in the electrostatic potential of the threefold channels in Fer147 and the fourfold channels in PeFer suggests significant diversity between Fer147 and PeFer in terms of metal ion aggregation and cation exclusion. In summary, the presented crystal structures may serve as references for studies of the iron‐storage mechanism of additional ferritins from marine invertebrates.

show abstract

The unusual co-assembly of H- and M-chains in the ferritin molecule from the Antarctic teleosts Trematomus bernacchii and Trematomus newnesi

Cited by 50 publications

References 26 publications

Role of H-1 and H-2 Subunits of Soybean Seed Ferritin in Oxidative Deposition of Iron in Protein

Role of H-1 and H-2 Subunits of Soybean Seed Ferritin in Oxidative Deposition of Iron in Protein

Genome-wide comparison of ferritin family from Archaea, Bacteria, Eukarya, and Viruses: its distribution, characteristic motif, and phylogenetic relationship

Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta

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