Transcriptional regulation of the matrix protein Shematrin-2 during shell formation in pearl oyster
نویسندگان
چکیده
منابع مشابه
Dual Roles of the Lysine-Rich Matrix Protein (KRMP)-3 in Shell Formation of Pearl Oyster, Pinctada fucata
Matrix proteins play important roles in shell formation. Our group firstly isolated three cDNAs encoding lysine-rich matrix protein from Pinctada fucata in 2006. However, the functions of KRMPs are not fully understood. In addition, KRMPs contain two functional domains, the basic domain and the Gly/Tyr domain respectively. Based on the modular organization, the roles of their two domains were p...
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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 c...
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Mollusk shell formation is a fascinating aspect of biomineralization research. Shell matrix proteins play crucial roles in the control of calcium carbonate crystallization during shell formation in the pearl oyster, Pinctada fucata. Characterization of biomineralization-related genes during larval development could enhance our understanding of shell formation. Genes involved in shell biomineral...
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In this study, we analyzed the combined effect of microalgal concentration and temperature on the shell growth of the bivalve Pinctada margaritifera and the molecular mechanisms underlying this biomineralization process. Shell growth was measured after two months of rearing in experimental conditions, using calcein staining of the calcified structures. Molecular mechanisms were studied though t...
متن کاملRapid evolution of pearl oyster shell matrix proteins with repetitive, low-complexity domains.
The lysine (K)-rich mantle protein (KRMP) and shematrin protein families are unique to the organic matrices of pearl oyster shells. Similar to other proteins that are constituents of tough, extracellular structures, such as spider silk, shematrins and KRMPs, contain repetitive, low-complexity domains (RLCDs). Comprehensive analysis of available gene sequences in three species of pearl oyster us...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2018
ISSN: 0021-9258
DOI: 10.1074/jbc.ra118.005281