Cloning and Characterization of a Heterogeneous Nuclear Ribonucleoprotein Homolog from Pearl Oyster, Pinctada fucata

• 来源期刊: 生物化学与生物物理学报（英文版）
• 关键词: RNA-recognition motif heterogeneous nuclear ribonucleoprotein glycine-rich protein Pinctada fucata
• 年，卷（期）: 2007,（12）
• 页码范围: 955-963
• 页数: 9页
• 语种: 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.