Cloning and identification of a YY-1 homolog as a potential transcription factor from Pinctada fucata.

Cloning and identification of a YY-1 homolog as a potential transcription factor from Pinctada fucata.
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DOI:
10.1016/j.gene.2015.07.003
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发表时间:
2015-11
期刊:
影响因子:
3.5
通讯作者:
Xiangnan Zheng;Minzhang Cheng;Liang Xiang;Jingtan Su;Yujuan Zhou;L. Xie;Rongqing Zhang
Xiangnan Zheng;Minzhang Cheng;Liang Xiang;Jingtan Su;Yujuan Zhou;L. Xie;Rongqing Zhang
中科院分区:
生物学3区
文献类型:
--
作者:
Xiangnan Zheng;Minzhang Cheng;Liang Xiang;Jingtan Su;Yujuan Zhou;L. Xie;Rongqing Zhang

文献摘要

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生物矿化是生物体内普遍存在的重要过程。软体动物的壳形成是一种典型的生物矿物物理活动,是生物矿化研究的典型模型。最近的研究主要集中在鉴定参与壳形成的基质蛋白;然而,对它们的转录调控机制,特别是参与壳形成的转录因子知之甚少。在本研究中,我们从凤尾莲中鉴定出一个与YY-1转录因子同源的基因,命名为pf -YY-1,并对其表达模式和生物学功能进行了表征。pf - yy -1具有与人类、小鼠和其他高等生物高度相似的典型锌指基序,这表明其具有dna结合能力和转录因子功能。pf - yy -1在许多组织中普遍表达,但在地幔中表达的水平较高,这表明它在生物矿化中起作用。在珍珠囊发育过程中,pf - y -1的表达模式与prisilkin -39、ACCBP等生物矿化相关基因的表达模式非常相似,并与之同步,也提示其在生物矿化过程中具有一定的功能。
Biomineralization is an important and ubiquitous process in organisms. The shell formation of mollusks is a typical biomineral physical activity and is used as a canonical model in biomineralization research. Most recent studies focused on the identification of matrix proteins involved in shell formation; however, little is known about their transcriptional regulation mechanism, especially the transcription factors involved in shell formation. In this study, we identified a homolog of the YY-1 transcriptional factor from Pinctadafucata, namedPf-YY-1, and characterized its expression pattern and biological functions.Pf-YY-1has a typical zinc finger motif highly similar to those in humans, mice, and other higher organisms, which indicated its DNA-binding capability and its function as a transcription factor.Pf-YY-1is ubiquitously expressed in many tissues, but at a higher level in the mantle, which suggested a role in biomineralization. The expression pattern ofPf-YY-1during pearl sac development was quite similar to, and was synchronized with, those ofPrisilkin-39,ACCBP, and other genes involved in biomineralization, which also suggested its function in biomineralization.