碳酸钙
互补DNA
氨基酸
打开阅读框
信号肽
肽序列
化学
病毒基质蛋白
生物矿化
生物
信使核糖核酸
生物化学
基因
古生物学
有机化学
作者
Xiaojun Liu,Zhenming Liu,Can Jin,Haoran Li,Jiale Li
摘要
Abstract Matrix proteins play important roles in molluscan shell biomineralization, which helps in the understanding of mechanisms associated with pearl formation. In this study, we characterized the gene encoding a novel shell‐matrix protein, hic24 , in Hyriopsis cumingii and investigated its structure and function. The full cDNA sequence of hic24 is 756 bp, with an open reading frame of 654 bp encoding 217 amino acids, including a signal peptide of 18 amino acids. Sequence analysis revealed that the protein is ∼23.5 kDa, and that Gly accounted for 11.5% of the total amino acid content. Secondary structure prediction indicated a structure comprised predominantly by β‐folds. Quantitative real‐time polymerase chain reaction and in situ hybridization indicated that hic24 is expressed in the dorsal epithelial cells of the mantle, indicating hic24 as a nacreous‐layer matrix protein. Additionally, hic24 expression patterns during pearl biomineralization showed that hic24 regulates the growth of the later nacreous layer. After attenuating hic24 expression by RNA interference in the mantle, we observed that hic24 plays a role in biomineralization of the shell nacre by inhibiting calcium carbonate nucleation.
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