Pan Chunqing, Zhao Heng, Shen Lin, Sheng Jiping
College of Food Sciences, China Agricultural University, Beijing 100080, China; E-Mails:
Int J Mol Sci. 2011;12(6):3797-809. doi: 10.3390/ijms12063797. Epub 2011 Jun 9.
Members of tripartite motif (TRIM) proteins in mammals play important roles in multiple cellular processes in the immune system. In the present study we have obtained the chicken TRIM39 with the insertion of a base A at position 1006 bp, compared to the sequence in the NCBI database (Accession No: NM 001006196), which made TRIM39 fulfill the TRIM rule of domain composition with both PRY, and SPRY domains. The open reading frame consisted of 1392 bp encoding 463 amino acid residues. The amino acid sequences of TRIM39 protein in mammals were highly similar (from 91.48% to 99.61%), while chicken TRIM39 had relatively low homology with mammals (from 29.2% to 39.59%). Real time RT-PCR indicated that the mRNA expression level of TRIM39 was the highest in spleen, with a lower expression in liver, brain, and lung, suggesting it might be an important protein participating in the immune system.
哺乳动物中的三方基序（TRIM）蛋白成员在免疫系统的多种细胞过程中发挥着重要作用。在本研究中，我们获得了鸡的TRIM39，与NCBI数据库中的序列（登录号：NM 001006196）相比，其在1006 bp处插入了一个碱基A，这使得TRIM39满足了具有PRY和SPRY结构域的TRIM结构域组成规则。开放阅读框由1392 bp组成，编码463个氨基酸残基。哺乳动物中TRIM39蛋白的氨基酸序列高度相似（从91.48%到99.61%），而鸡的TRIM39与哺乳动物的同源性相对较低（从29.2%到39.59%）。实时RT-PCR表明，TRIM39的mRNA表达水平在脾脏中最高，在肝脏、大脑和肺中的表达较低，表明它可能是参与免疫系统的一种重要蛋白质。
