Protein Association and Dissociation Regulated by Ferric Ion

Li, Chaorui; Fu, Xiaoping; Qi, Xin; Hu, Xiaosong; Chasteen, N. Dennis; Zhao, Guanghua

doi:10.1074/jbc.m109.011528

Cited by 59 publications

(38 citation statements)

References 39 publications

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“…Both excitation and emission wavelengths were set to 680 nm, and the time-dependent change in scattering light was set to a 90°angle, perpendicular to the beam, and recorded as previously reported (13). All quoted concentrations are final concentrations after mixing the two reagents.…”

Section: Methodsmentioning

confidence: 99%

“…Preparation of WT SSF, rH-1, rH-2, and rH-1H-2-SSF was purified as recently described (8,13). rH-1 was prepared according to reported methods (8,18).…”

Section: Methodsmentioning

confidence: 99%

“…Preparation of rH-1, rH-2, and WT SSF with EP DeletedThe preparations of EP-deleted rH-1, rH-2, and WT SSF were carried out as described recently (13,14). Purified holophytoferritin (3.0 mg) was added to 0.24 ml of Alcalase 2.4 L (Novozymes, Denmark) and incubated at 60°C for 5 min, followed by phenylmethanesulfonyl fluoride at a final concentration of 2 mM to stop the proteolysis reaction.…”

Section: Methodsmentioning

confidence: 99%

“…The crystal structure of recombinant SSF shows that the EP is located on the exterior surface of protein and stabilizes the entire oligomeric conformation of phytoferritin by its interaction with a neighboring subunit on the shell surface (12). Recent studies of our group reveal the role of the EP during iron oxidative deposition in phytoferritin as the second binding and ferroxidase center that contributes to mineralization of the iron core at high iron loading of ferritin (Ͼ48 irons/shell) (13). On the other hand, the EP exhibits a significant serine protease-like activity (14), which is responsible for protein autodegradation during seed germination (14 -16).…”

mentioning

confidence: 99%

“…At low iron loading of apoferritin (Յ48 irons/protein shell, 2 irons/subunit), no protein association occurs with both recombinant soybean seed H-1 (rH-1) and H-2 (rH-2) ferritins, indicating that iron oxidation occurs only through the diiron ferroxidase mechanism (13). Once the binding capacity of the 24 ferroxidase centers (48 irons/shell) is exceeded, the oxidative addition of Fe 2ϩ to the aporH-2 to form Fe 3ϩ causes protein aggregation, whereas such protein association is not observed in its analog, rH-1, until the amount of added iron is increased to 300 Fe 2ϩ /protein shell.…”

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confidence: 99%

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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: Methodsmentioning

confidence: 99%

“…Preparation of WT SSF, rH-1, rH-2, and rH-1H-2-SSF was purified as recently described (8,13). rH-1 was prepared according to reported methods (8,18).…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

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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The extension peptide of plant ferritin from sea lettuce contributes to shell stability and surface hydrophobicity

et al. 2012

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Plant ferritins have some unique structural and functional features. Most of these features can be related to the plant-specific ''extension peptide" (EP), which exists in the Nterminus of the mature region of a plant ferritin. Recent crystallographic analysis of a plant ferritin revealed the structure of the EP, however, two points remain unclear: (i) whether the structures of well-conserved EP of plant ferritins are common in all plants, and (ii) whether the EP truly contributes to the shell stability of the plant ferritin oligomer. To clarify these matters, we have cloned a green-plant-type ferritin cDNA from a green alga, Ulva pertusa, and investigated its crystal structure. Ulva pertusa ferritin (UpFER) has a plant-ferritin-specific extension peptide composed of 28 amino acid residues. In the crystal structure of UpFER, the EP lay on and interacted with the neighboring threefold symmetry-related subunit. The amino acid residues involved in the interaction were very highly conserved among plant ferritins. The EPs masked the hydrophobic pockets on the ferritin shell surface by lying on them, and this made the ferritin oligomer more hydrophilic. Furthermore, differential scanning calorimetric analysis of the native and its EP-deletion mutant suggested that the EP contributed to the thermal stability of the plant ferritin shell. Thus, the shell stability and surface hydrophobicity of plant ferritin were controlled by the presence or absence of the plant-ferritin-specific EP. This regulation can account for those processes such as shell stability, degradation, and association of plant ferritin, which are significantly related to iron utilization in plants.

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The Size Flexibility of Ferritin Nanocage Opens a New Way to Prepare Nanomaterials

Zhang

Zang

Chen

et al. 2017

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Ferritins are ubiquitous iron storage proteins where Fe(II) sequestration prevents not only its spontaneous oxidation to Fe(III) but also production of toxic free radicals. Recently, scientists have subverted these nature functions and used ferritin cage structures of nanometer dimensions for encapsulation of guest molecules such as anti-cancer drugs or bioactive nutrients based on pH induced ferritin disassembly and reassembly property. However, prior to this study, ferritin nanocage was required to disassemble only under harsh pH conditions (≤2.0 or ≥11.0), followed by reassembly at near neutral pH. Such harsh conditions can cause protein or guest molecules damage to a great extent during this pH-induced unfolding-refolding process. Here, we provide evidence demonstrating that the apoferritin shell is flexible rather than rigid. Indeed, we found that two large complex molecules, uranyl acetate dihydrate and phosphotungstic acid, can reach the cavity of both plant and animal apoferritin followed by mineralization. Moreover, large organic compound such as curcumin and doxorubicin can also be encapsulated within ferritin cavity by its mixing with protein. This strategy will increase the use of ferritin in nanotechnology, and could be also applicable to other shell-like proteins as templates to prepare nanomaterials.

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Protein Association and Dissociation Regulated by Ferric Ion

Cited by 59 publications

References 39 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

The extension peptide of plant ferritin from sea lettuce contributes to shell stability and surface hydrophobicity

The Size Flexibility of Ferritin Nanocage Opens a New Way to Prepare Nanomaterials

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