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The structure–function relationship analysis of Prismalin‐14 from the prismatic layer of the Japanese pearl oyster, Pinctada fucata
Author(s) -
Suzuki Michio,
Nagasawa Hiromichi
Publication year - 2007
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2007.06036.x
Subject(s) - pinctada fucata , calcium carbonate , chitin , recombinant dna , amino acid , chemistry , biochemistry , calcium , peptide sequence , in vitro , carbonate , stereochemistry , biology , chitosan , pearl oyster , pearl , gene , organic chemistry , philosophy , theology
The mollusk shell is a hard tissue consisting of calcium carbonate and organic matrices. The organic matrices are considered to play important roles in shell formation. We have previously identified a prismatic layer‐specific protein named Prismalin‐14, which consists of 105 amino acid residues and includes four structurally characteristic regions; a repeated sequence of Pro‐Ile‐Tyr‐Arg, a Gly/Tyr‐rich region and N‐ and C‐terminal Asp‐rich regions. Prismalin‐14 showed an inhibitory activity on calcium carbonate precipitation and a calcium‐binding ability in vitro . In this study, we prepared some molecular species of recombinant proteins including Prismalin‐14 and its truncated proteins in an Escherichia coli expression system to reveal a structure–function relationship of Prismalin‐14. The results showed that the Gly/Tyr‐rich region was responsible for chitin binding and was identified as a novel chitin‐binding sequence. On the other hand, both N‐ and C‐terminal Asp‐rich regions are related to inhibitory activity on calcium carbonate precipitation in vitro . Immunohistological observation revealed that Prismalin‐14 was localized at the acid‐insoluble organic framework including chitin. All these results strongly suggest that Prismalin‐14 is a framework protein that mediates chitin and calcium carbonate crystals by using its acidic and chitin‐binding regions.