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

• 作 者: Xunhao XIONG Qiaoli FENG Liping XIE Rongqing ZHANG
• 机 构: Institute of Marine Biotechnology,Department of Biological Science and Biotechnology,Tsinghua Univer
• 出 处: 生物化学与生物物理学报（英文版）
• 发表日期: 2007年12期
• 关键词: RNA-recognition motif heterogeneous nuclear ribonucleoprotein glycine-rich prote

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 patte 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.