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Molecular Cloning and Distribution of a Plasma Membrane Calcium ATPase Homolog from the Pearl Oyster Pinctadafucata

ISSN号：1000-3282
期刊名称：《生物化学与生物物理进展》
时间：0
分类：Q51[生物学—生物化学]
作者机构：[1]Institute of Marine Biotechnology, Department of Biological Science and Biotechnology, Tsinghua University, Beijing 100084, China, [2]Protein Science Laboratory of the Ministry of Education, Tsinghua University, Beijing 100084, China
相关基金：This work was supported by the grants from the National Natural Science Foundation of China （30530600, 30371092 and 30221003）

关键词： RNA识别基因, 核蛋白, 氨基乙酸, 生物化学, RNA-recognition motif, heterogeneous nuclear ribonucleoprotein, glycine-rich protein, Pinctada fucata

中文摘要：

异构的原子 ribonucleoproteins (hnRNPs ) 在基因表达的 post-transcriptional 有基本角色。这里，编码假定全身的 RNA 有约束力的蛋白质的 cDNA 与 cDNA 结束的退化教材，和快速的扩大用反向的抄写聚合酶链反应从珍珠牡蛎(Pinctada fucata ) 被孤立。全身的 cDNA 与与 8.7 的 69 kDa 和等电点的预言的分子的重量编码 624 氨基酸的蛋白质的一个开的读物框架由 2737 bp 组成。RNA 有约束力的蛋白质介绍的通常认为的珍珠牡蛎分子的组织结束到 hnRNPs，也就是，酸的 N 终端由包含 RG/RGG 的三个 RNA 识别主题和 C 终端列在后面重复主题。什么时候 transfected HeLa 房间，基因表达产品仅仅在原子核被发现的 Pf-HRPH (Pinctada fucata hnRNP 相当或相同的事物) ，表明它是原子蛋白质。表示模式被量的即时聚合酶链反应也调查，显示 Pf-HRPH mRNA 富有地在性腺，鳃，和内脏被表示。根据我们知道，通常认为的 Pf-HRPH 是在软体动物克隆的第一个 hnRNP 相当或相同的事物。这些数据为 RNA 有约束力的蛋白质的多重函数的进一步的学习是重要的。

英文摘要：

Heterogeneous nuclear ribonucleoproteins （hnRNPs） have fundamental roles in the posttranscriptional control of gene expression. Here, a cDNA encoding a presumed full-length RNA-binding protein was isolated from pearl oyster （Pinctadafucata） using reverse transcription-polymerase chain reaction with degenerate primers, and rapid amplification of cDNA ends. The full-length cDNA consists of 2737 bp with an open reading frame encoding a protein of 624 amino acids with a predicted molecular weight of 69 kDa and isoelectric point of 8.7. The putative pearl oyster RNA-binding protein presents a molecular organization close to the hnRNPs, namely an acidic N-terminal followed by three RNA-recognition motifs and a Cterminal that contains RG/RGG repeated motifs. When transfected HeLa cells, the Pf-HRPH （Pinctada fucata hnRNP homolog） gene expression product was found only in nuclei, revealing that it is a nuclear protein. The expression pattern was also investigated by quantitative real-time polymerase chain reaction, indicating that Pf-HRPH mRNA was abundantly expressed in gonad, gill, and viscera. As far as we know, the putative Pf-HRPH is the first hnRNP homolog cloned in mollusks. These data are significant for further study of the multiple functions of RNA-binding protein.