Silkmapin of Hyriopsis cumingii, a novel silk-like shell matrix protein involved in nacre formation

Gene. 2015 Jan 25;555(2):217-22. doi: 10.1016/j.gene.2014.11.006. Epub 2014 Nov 7.

Abstract

Understanding the role of matrix proteins in nacre formation and biomineralization in mollusks is important for the pearl industry. In this study, the gene encoding the novel Hyriopsis cumingii shell matrix protein silkmapin was characterized. The gene encodes a protein of 30.89kDa in which Gly accounts for 34.41% of the amino acid content, and the C-terminal region binds Ca(2+). Secondary structure prediction indicated a predominantly β-fold and a structure typical of filamentous proteins. Real-time quantitative PCR and in situ hybridization showed that silkmapin was expressed in epithelial cells at the edge and pallial of mantle tissue, indicated that silkmapin play roles in the shell nacreous and prismatic layer formation. Further real-time PCR results indicated an involvement in pearl formation via nucleation of calcium carbonate prior to formation of the nacre.

Keywords: Biomineralization; Freshwater mussel; Hyriopsis cumingii; Matrix protein; Nacre.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animal Shells / metabolism*
  • Animals
  • Base Sequence
  • Calcium / metabolism
  • Calcium Carbonate / metabolism*
  • Cloning, Molecular
  • Gene Expression Regulation
  • Molecular Sequence Data
  • Nacre / metabolism*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Proteins / metabolism*
  • Real-Time Polymerase Chain Reaction
  • Silk / metabolism*
  • Unionidae / metabolism*

Substances

  • Nacre
  • Proteins
  • Silk
  • Calcium Carbonate
  • Calcium