Characterization and function of a novel calmodulin-like protein from crayfish Procambarus clarkii

Calmodulin plays an important role in calcium-dependent signal transduction pathways. In this experiment, a novel calmodulin-like gene (Pc-CaM-L) was identified in the crayfish Procambarus clarkii; it encodes a polypeptide of 145 amino acids. Quantitative real-time PCR analysis revealed that Pc-CaM-L was expressed in all examined tissues, including hepatopancreas, hemocytes, heart, gill, intestine and muscle; the highest Pc-CaM-L expression level was detected in the hepatopancreas. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and western blot analysis demonstrated that a recombinant Pc-CaM-L protein was successfully expressed in Escherichia coli. The calcium-binding activity of the purified Pc-CaM-L protein was confirmed by gel mobility shift assay. The expression of Pc-CaM-L was significantly upregulated in gut, gill and hemocytes after lipopolysaccharide or polyinosinic:polycytidylic acid induction. These results suggest that Pc-CaM-L plays a role in the immune response of P. clarkii.