Abstract
In the present study, we describe the purification and molecular characterization of Cu,Zn superoxide dismutase (SOD) from Chionodraco hamatus, an Antarctic teleost widely distributed in many areas of the Ross Sea that plays a pivotal role in the Antarctic food chain. The primary sequence was obtained using biochemical and molecular biology approaches and compared with Cu,Zn SODs from other organisms. Multiple sequence alignment using the amino acid sequence revealed that Cu,Zn SOD showed considerable sequence similarity with its orthologues from various vertebrate species, but also some specific substitutions directly linked to cold adaptation. Phylogenetic analyses presented the monophyletic status of Antartic Teleostei among the Perciformes, confirming the erratic differentiation of these proteins and concurring with the theory of the “unclock-like” behavior of Cu,Zn SOD evolution. Expression of C. hamatus Cu,Zn SOD at both the mRNA and protein levels were analyzed in various tissues, highlighting the regulation of gene expression related to environmental stress conditions and also animal physiology. The data presented are the first on the antioxidant enzymes of a fish belonging to the Channichthyidae family and represent an important starting point in understanding the antioxidant systems of these organisms that are subject to constant risk of oxidative stress.
Highlights
Various proteins and compounds defend cells from reactive oxygen species (ROS)
SOD1s from many fish have been characterized [9,10,11], very limited knowledge exists regarding this protein in Antarctic fish [12] and nothing is known of those belonging to the Channichthyidae family, the icefish
We describe the molecular characterization of SOD1 from Chionodraco hamatus, a teleost living in the cold waters surrounding the Antarctic continental shelf
Summary
Various proteins and compounds defend cells from reactive oxygen species (ROS). Superoxide dismutases (SODs, EC 1.15.1.1) are metalloenzymes with the main physiological role of preventing oxidative stress by catalyzing the partitioning of the superoxide anion ( O2 − ) into hydrogen peroxide and molecular oxygen [1,2].In animals, there are three known types of SODs: manganese SOD (Mn SOD or SOD2), which is localized in the mitochondrial matrix, and two Cu,Zn SODs, namely intracellular SOD (IC SOD or SOD1) and extracellular SOD (EC SOD or SOD3) with respect to their cellular localization [3,4].Antioxidants 2020, 9, 325; doi:10.3390/antiox9040325 www.mdpi.com/journal/antioxidantsCu,Zn SODs show extremely conserved structural and functional parameters, such as their kinetics and their electrostatic potential surrounding the active site, a feature that modulates the catalytic mechanism of these enzymes [5,6]. Superoxide dismutases (SODs, EC 1.15.1.1) are metalloenzymes with the main physiological role of preventing oxidative stress by catalyzing the partitioning of the superoxide anion ( O2 − ) into hydrogen peroxide and molecular oxygen [1,2]. SOD1s from many fish have been characterized [9,10,11], very limited knowledge exists regarding this protein in Antarctic fish [12] and nothing is known of those belonging to the Channichthyidae family, the icefish. We describe the molecular characterization of SOD1 from Chionodraco hamatus, a teleost living in the cold waters surrounding the Antarctic continental shelf. We employed in silico approaches to investigate Antarctic fish SOD1s for the possible presence of molecular cold adaptation characteristics
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