Document Type : Original Article
Key Laboratory of the Ministry of Education for Applied Marine Biotechnology, School of Marine, Ningbo University, Fenghua Rd. 818, Ningbo, 315211, Zhejiang, People’s Republic of China
Collaborative Innovation Center for Zhejiang Marine High-Efficiency and Healthy Aquaculture, Ningbo University, Ningbo, People’s Republic of China
The aim of this work was to investigate the function of the peroxiredoxin family member Peroxiredoxin 6 in Sepiella maindroni (Smprx6) during embryonic development and the response to thermal stress. The 1064 bp full-length coding sequence of Smprx6 includes an open reading frame of 660 bp encoding a polypeptide of 219 amino acids with a predicted molecular mass of 24.4 kDa. The deduced protein sequence shares significant homology with other reported Prx6 enzymes. Phylogenetic analysis classified SmPrx6 into the 1-Cys-Prx cluster, and quantitative real-time PCR (qPCR) demonstrated constitutive mRNA expression in all tested tissues and during five different embryonic developmental stages, as previously documented in other cephalopods. Thermal stress induced Smprx6 expression, which peaked at 6 h then returned to control levels. Recombinant SmPrx6 was active at different concentrations and was thiol-dependant. The results suggest that SmPrx6 plays a major role in the development of Sepiella maindroni and its response to oxidative and thermal stress.