Middle ferritin genes from the icefish Chionodraco rastrospinosus: Comparative analysis and evolution of fish ferritins

Scudiero, Rosaria; Esposito, Maria; Trinchella, Francesca

doi:10.1016/j.crvi.2013.03.003

Cited by 12 publications

(2 citation statements)

References 34 publications

(53 reference statements)

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“…H-subunit typically contains a di-iron ferroxidase center capable of rapidly oxidizing ferrous (Fe 2+ ) ions, whereas the L-subunit lacks such ferroxidase center but does have a nucleation site ( Pozzi et al, 2017 ). Ferritins from lower vertebrate (e.g., bullfrogs and fish) and invertebrate species dispose with a third subunit type, named the Hʹ-subunit, which harbors the residues forming both the ferroxidase center and the nucleation site ( Domínguez-Vera et al, 2010 ; Scudiero et al, 2013 ; Pozzi et al, 2015b ). However, the biological structures and catalytic characteristics of marine invertebrate ferritins and their iron translocation pathways remain relatively unknown.…”

Section: Introductionmentioning

confidence: 99%

Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa

Ming

Jiang

Huo

et al. 2022

Front. Mol. Biosci.

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In addition to its role as an iron storage protein, ferritin can function as a major detoxification component in the innate immune defense, and Cu2+ ions can also play crucial antibacterial roles in the blood clam, Tegillarca granosa. However, the mechanism of interaction between iron and copper in recombinant Tegillarca granosa ferritin (TgFer) remains to be investigated. In this study, we investigated the crystal structure of TgFer and examined the effects of Fe2+ and Cu2+ ions on the TgFer structure and catalytic activity. The crystal structure revealed that TgFer presented a typically 4–3–2 symmetry in a cage-like, spherical shell composed of 24 identical subunits, featuring highly conserved organization in both the ferroxidase center and the 3-fold channel. Structural and biochemical analyses indicated that the 4-fold channel of TgFer could be serviced as potential binding sites of metal ions. Cu2+ ions appear to bind preferentially with the 3-fold channel as well as ferroxidase site over Fe2+ ions, possibly inhibiting the ferroxidase activity of TgFer. Our results present a structural and functional characterization of TgFer, providing mechanistic insight into the interactions between TgFer and both Fe2+ and Cu2+ ions.

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Section: Introductionmentioning

confidence: 99%

Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa

Ming

Jiang

Huo

et al. 2022

Front. Mol. Biosci.

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“…In fish, M ferritin has been identified in a number of species including Oplegnathus fasciatus, Chionodraco rastrospinosus, Epinephelus bruneus, Cynoglossus semilaevis, Scophthalmus maximus, Pseudosciaena crocea, Trematomus bernacchii, and Salmo salar (Andersen et al 1995(Andersen et al , 1998Mignogna et al 2002;Giorgi et al 2008;Zhang et al 2010;Harikrishnan et al 2011;Wang et al 2011;Elvitigala et al 2013;Scudiero et al 2013;Lee et al 2014). However, only a few of these ferritins were shown to possess iron binding and/or antioxidative potential.…”

Section: Introductionmentioning

confidence: 95%

Ferritin M of Paralichthys olivaceus possesses antimicrobial and antioxidative properties

Wang

Sun

2015

Fish Physiol Biochem

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Ferritin is an evolutionarily conserved protein that plays a vital role in maintaining iron homeostasis. In this study, we identified a ferritin M (PoFerM) from Japanese flounder (Paralichthys olivaceus) and analyzed its biological property. PoFerM is composed of 176 amino acid residues and contains the conserved ferroxidase diiron center and the ferrihydrite nucleation center typical of M ferritins. Expression of PoFerM occurred in multiple tissues and was most abundant in blood. Bacterial infection upregulated PoFerM expression in head kidney, spleen, and liver in a time-dependent manner. Recombinant PoFerM (rPoFerM) purified from Escherichia coli exhibited iron-chelating activity and inhibited bacterial growth, whereas rPoFerMM, the mutant protein that bears alanine substitution at two conserved residues of the ferroxidase center and the ferrihydrite nucleation center, failed to do so. Oxidative protection analysis showed that rPoFerM, but not rPoFerMM, was able to alleviate the deleterious effect of H2O2-induced free radicals on plasmid DNA and primary flounder cells. Together these results indicate that PoFerM is an iron chelator with antimicrobial and antioxidative properties, all which depend on the conserved ferroxidase center and the ferrihydrite nucleation site.

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A ferritin gene in the marine copepod Acartia tonsa as a highly sensitive biomonitor for nano-contamination

2022

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Middle ferritin genes from the icefish Chionodraco rastrospinosus: Comparative analysis and evolution of fish ferritins

Cited by 12 publications

References 34 publications

Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa

Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa

Ferritin M of Paralichthys olivaceus possesses antimicrobial and antioxidative properties

A ferritin gene in the marine copepod Acartia tonsa as a highly sensitive biomonitor for nano-contamination

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