Structural and functional analysis of ferritin heavy chain subunit in Oryziaslatipes

Abstract

In North East region of India, iron toxicity is one of the major problems in culture fisheries. To overcome this challenge, it is necessary to identify the role of ferritin protein as an iron detoxificant and store in fishes. The Heavy chain in a ferritin protein possess di- Fe binding site in the fourth helix that interacts with oxygen. In this paper attempt has been made to study the structure and function of ferritin heavy chain subunit of Oryzias latipes from amino acid sequence. Physicochemical characterization by Expasy ProtParam form tools reveals that the protein is acidic, unstable and hydrophilic. A hydropathy scale showed two peak with significant score above the threshold value (0 to + value) but TMHMM conclude that there were one transmembrane domain within protein. The secondary structures contain alpha helix (56.50%), extended strands (10.73%) and coiled region (32.77%). The query sequence shows homology to the selected template (structure of mouse heavy chain modified ferritin by X-ray diffraction technique) with maximum % identity. To analyse the phylogenetic relationship, ML tree was constructed between Oryzias latipes and Oryzias melastigma for the ferritin heavy sub unit along with Cyprinus carpio as out crossed. Two distinct clads formation was observed between same genus species and the out crossed species. In protein-protein interaction analysis via STRING 10.0 tool, two enriched pathways of KEGG, six Inter Pro domains, one PFAM protein domain, one Uniprot keywords and eleven functional parameters of network analysis were identified in Oryzias latipes. The overall investigation reveals the structural features and their association in detoxification and iron homeostasis. Keywords: Ferritin Heavy Chain; Oryzias latipes; Physicochemical Characterization; Homology Modeling