Molecular profiling and functional insights of rock bream (Oplegnathus fasciatus) thioredoxin reductase 3-like molecule: investigation of its transcriptional modulation in response to live pathogen stress.

摘要: Abstract The thioredoxin (Trx) system plays a significant role in cellular antioxidative defense by dismutating the surpluses of reactive oxygen species. Thus, reductase (TrxR) cannot be ignored, owing to its participation initiating Trx enzyme cascade. Here, we report identification and molecular characterization teleostean TrxR (RbTrxR-3) ortholog that showed high similarity with TrxR-3 isoforms other vertebrates. complete RbTrxR-3 coding sequence comprised 1800 nucleotides, encoding 600-amino acid protein predicted mass ~ 66 kDa. consisted 16 exons separated 15 introns had total length 12,658 bp. In silico analysis revealed it possesses typical domain architecture. Moreover, using multiple alignment pairwise strategies, has overall proteins, including highly conserved active site residues. Phylogenetic reconstruction affirmed close evolutionary relationship fish orthologs, as indicated clustering pattern. transcriptional analysis, performed quantitative polymerase chain reaction (qPCR), was ubiquitously distributed, highest level mRNA expression blood, followed gill, liver. Live bacterial viral stimuli triggered modulation basal transcription liver tissues correlated temporally putative substrate, rock bream thioredoxin1 under same conditions pathogenic stress. Finally, resembling function protein, purified recombinant detectable dose-dependent thiol activity against 5,5′-dithiobis (2-nitrobenzoic) acid. Taken together, these results suggest host oxidative