Peroxiredoxin 6 from cuttlefish (Sepiella maindroni): molecular characterisation during development and the response to thermal stress

Abstract

The aim of this work was to investigate the function of the peroxiredoxin family member Peroxiredoxin 6 in <em>Sepiella maindroni</em> (<em>Smprx6</em>) during embryonic development and the response to thermal stress. The 1064 bp full-length coding sequence of <em>Smprx6</em> 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 <em>Smprx6</em> 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 <em>Sepiella maindroni</em> and its response to oxidative and thermal stress.