Abstract

The shell of the pearl oyster (Pinctada fucata) mainly comprises aragonite whereas that of the Pacific oyster (Crassostrea gigas) is mainly calcite, thereby suggesting the different mechanisms of shell formation between above two mollusks. Calmodulin (CaM) is an important gene for regulating the uptake, transport, and secretion of calcium during the process of shell formation in pearl oyster. It is interesting to characterize the CaM in oysters, which could facilitate the understanding of the different shell formation mechanisms among mollusks. We cloned the full-length cDNA of Pacific oyster CaM (cgCaM) and found that the cgCaM ORF encoded a peptide of 113 amino acids containing three EF-hand calcium-binding domains, its expression level was highest in the mantle, hinting that the cgCaM gene is probably involved in shell formation of Pacific oyster, and the common ancestor of Gastropoda and Bivalvia may possess at least three CaM genes. We also found that the numbers of some EF hand family members in highly calcified species were higher than those in lowly calcified species and the numbers of these motifs in oyster genome were the highest among the mollusk species with whole genome sequence, further hinting the correlation between CaM and biomineralization.

Highlights

  • Calmodulin (CaM) seems to play important roles in regulating the uptake, transport, and secretion of calcium in molluscan shell formation, such as yesso scallop (Patinopecten yessoensis) [1], freshwater pearl mussel (Hyriopsis schlegelii) [2], and pearl oyster (Pinctada fucata) [3]

  • PfCaM and pfCaLP are believed to play important roles in shell formation of the pearl [10, 11] oyster and it was concluded that cgCaM may play a different role in shell formation by the Pacific oyster because the composition of the Pacific oyster shell is different from that of the pearl oyster

  • We found that the cgCaM gene expression level was highest in the mantle, thereby suggesting that its function is probably related to shell formation

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Summary

Introduction

Calmodulin (CaM) seems to play important roles in regulating the uptake, transport, and secretion of calcium in molluscan shell formation, such as yesso scallop (Patinopecten yessoensis) [1], freshwater pearl mussel (Hyriopsis schlegelii) [2], and pearl oyster (Pinctada fucata) [3]. The pearl oyster CaM protein or calmodulin-like protein (CaLP) was found to interact with different target proteins in the mantle and the gill [4] and may regulate the calcite growth in the shell prismatic layer by inducing the aragonite nucleation and modifying the calcite morphology in vitro crystallization experiments [5]. The higher level of calcite in the oyster shell may suggest that CaM has a different function in the Pacific oyster. To elucidate the role of CaM in shell formation in the Pacific oyster, we cloned the full-length cDNA of Pacific oyster CaM (cgCaM) and analyzed its characteristics

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