Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus)

摘要: Ferritin is a conserved iron binding protein existing ubiquitously in prokaryotes and eukaryotes. In this study, the gene encoding ferritin M subunit homologue (SoFer1) was cloned from red drum (Sciaenops ocellatus) analyzed at expression functional levels. The open reading frame of SoFer1 531 bp preceded by 5'-untranslated region that contains putative Iron Regulatory Element (IRE) preserved many ferritins. deduced amino acid sequence possesses both ferroxidase center mammalian H nucleation site L ferritin. Expression tissue specific responded positively to experimental challenges with Gram-positive Gram-negative fish pathogens. Treatment liver cells iron, copper, oxidant significantly upregulated time-dependent manners. To further examine potential role antioxidation, transfected transiently were prepared. Compared control cells, transfectants exhibited reduced production reactive oxygen species following H(2)O(2) challenge. Finally, SoFer1. expressed purified Escherichia colt as recombinant protein. Iron-chelating analysis showed capable binding. Taken together, these results suggest likely be involved sequestration, host immune defence against bacterial infection, antioxidation. (C) 2010 Elsevier Ltd. All rights reserved.