Cloning and characterization of the shell matrix protein Shematrin in scallop Chlamys farreri.

The Shematrin family is unique to the organic matrices of pearl oyster shells, containing repetitive, low-complexity domains designated as XGnX (where X is a hydrophobic amino acid). Current studies suggested that Shematrins are framework proteins in the prismatic layer of Pinctada fucata; however, the exact function of Shematrin during shell formation is unclear. In this study, we cloned and characterized Shematrin, a protein highly homologous to Shematrin-2, from the mantle tissue of scallop (Chlamys farreri). Semi-quantitative reverse transcript polymerase chain reaction analysis showed that Shematrin is exclusively expressed in the mantle. Knocking down the expression of Shematrin in adult scallops via double-stranded RNA injection led to an abnormal folia surface. After the shell was notched, the expression level of Shematrin remarkably increased and then gradually decreased, suggesting that Shematrin is critically involved in the shell repair progress. Injection of Shematrin double-stranded RNA reduced the speed of shell regeneration and caused abnormal surface morphology of the regenerated shell. The RNA interference and shell notching experiments indicated that Shematrin plays a key role in the folia formation of C. farreri. Structure prediction showed that Shematrin may be an intrinsically disordered protein, with high flexibility and elasticity of the molecular conformation, which facilitate binding multiple protein partners. Based on the structure features, we hypothesized that Shematrin may participate in framework organization via binding with several specific acidic proteins, functioning as a molecular hub in the protein interaction networks.