Abstract
Ferritin has important functions in the transition and storage of toxic metal ions, but its regulation and function in many invertebrate species are still largely unknown. In our previous work, the cDNA sequence of Sinonovacula constricta, Apostichopus japonicas and Acaudina leucoprocta were constructed and efficiently expressed in E. Coli BL21 under IPTG induction. In this follow-up study, the recombinant ferritins were exposed to heavy metal manganese. The manganese concentration levels in three recombinant ferritins were greater than horse spleen ferritin (HSF). Compared with HSF, the amount of manganese enrichment in the three recombinant ferritins was 1.75-fold, 3.25-fold and 2.42-fold increases in ScFER, AjFER, and AlFER, respectively. After phosphate stimulation, the concentration of manganese increased and was higher than the ordinary dialysis control groups. The ScFER was four times its baseline value. The AjFER and AlFER were 1.4- and 8-fold higher, respectively. The AlFER sample stimulated by phosphate was 22-fold that of HSF. The morphologies of the resulting Mn-Ferritin from different marine invertebrates were characterized with scanning electron microscopy. Surface morphologies were lamella flower-like and are consistent with changes in surface morphologies of the standard Mn-HSF. Invertebrate recombinant ferritin and HSF both can uptake manganese. We found that the structure of A. leucoproctarecombinant Mn-Ferritin aggregate changed over time. The surface formed lamella flower-like aggregate, but gradually merged to create a relatively uniform plate-like phase of aggregate spherically and fused without clear boundaries.
Highlights
Ferritin is an iron-rich component first discovered in horse livers[1]
The molecular mass of the purified product was in good agreement with the predicted molecular weight of ScFER, AjFER, and AlFER
The intensity of the recombinant protein bands increased with time, and peak expression of recombinant ferritin occurred 5 h after IPTG was introduced
Summary
Ferritin is an iron-rich component first discovered in horse livers[1]. It is a highly conserved protein across animals, plants and microbes that stores and releases iron[2]. The first isolation of ferritin was facilitated by several distinct biochemical characteristics including its stability at PLOS ONE | DOI:10.1371/journal.pone.0119427. Recombinant Mn-Ferritin Flower-Like Spherical Aggregates high temperatures (80°C), relative insolubility in ammonium sulfate, and its crystallization with cadmium salts[3, 4]. Excess iron should be stored in ferritin to avoid iron poisoning. Ferritin releases iron to cells for bio-synthetic proteins or enzymes that utilize iron[5, 6]. Ferritin controls the amount of iron in the organism and has detoxification properties[7]
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