Identification of conserved proteins from diverse shell matrix proteome in Crassostrea gigas: Characterization of genetic bases regulating shell formation

The calcifying shell is an excellent model for studying biomineralization and evolution. However, the molecular mechanisms of shell formation are only beginning to be elucidated in Mollusca. It is known that shell matrix proteins (SMPs) play important roles in shell formation. With increasing data o...

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Bibliographic Details
Published in:Scientific Reports
Main Authors: Feng, D., Li, Q., Yu, H.
Format: Article in Journal/Newspaper
Language:English
Published: Nature Publishing Group 2017
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Online Access:http://hdl.handle.net/10713/11273
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85017012729&doi=10.1038%2fsrep45754&partnerID=40&md5=cba1ef655e54b5268ee586fc1d574ebe
https://doi.org/10.1038/srep45754
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Summary:The calcifying shell is an excellent model for studying biomineralization and evolution. However, the molecular mechanisms of shell formation are only beginning to be elucidated in Mollusca. It is known that shell matrix proteins (SMPs) play important roles in shell formation. With increasing data of shell matrix proteomes from various species, we carried out a BLASTp bioinformatics analysis using the shell matrix proteome from Crassostrea gigas against 443 SMPs from nine other species. The highly conserved tyrosinase and chitin related proteins were identified in bivalve. In addition, the relatively conserved proteins containing domains of carbonic anhydrase, Sushi, Von Willebrand factor type A, and chitin binding, were identified from all the ten species. Moreover, 25 genes encoding SMPs were annotated and characterized that are involved in CaCO 3 crystallization and represent chitin related or ECM related proteins. Together, data from these analyses provide new knowledge underlying the molecular mechanism of shell formation in C.gigas, supporting a refined shell formation model including chitin and ECM-related proteins. Copyright 2017 The Author(s). National Natural Science Foundation of China (31372524) https://doi.org/10.1038/srep45754